SPDH
目录号 : GC38342
SPDH 是一种可降解的 ADC 连接子，能应用于癌症或 B 细胞增生性疾病的诊断和治疗。
Cas No.:1824718-79-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
SPDH is a cleavable ADC linker used for diagnosis and treatment of cancer or B cell proliferative diseas.
| Cas No. | 1824718-79-7 | SDF | |
| Canonical SMILES | O=C(ON1C(CCC1=O)=O)CCCCCSSC2=NC=CC=C2 | ||
| 分子式 | C15H18N2O4S2 | 分子量 | 354.44 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 2.8214 mL | 14.1068 mL | 28.2135 mL |
| 5 mM | 0.5643 mL | 2.8214 mL | 5.6427 mL |
| 10 mM | 0.2821 mL | 1.4107 mL | 2.8214 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
The synpolydactyly homolog (SPDH) mutation in the mouse -- a defect in patterning and growth of limb cartilage elements
Mech Dev 2002 Mar;112(1-2):53-67.PMID:11850178DOI:10.1016/s0925-4773(01)00639-6.
We have investigated the recessive mouse mutant synpolydactyly homolog (SPDH) as a model for human synpolydactyly (SPD). As in human SPD, the SPDH phenotype consists of central polydactyly, syndactyly and brachydactyly and is caused by the expansion of a polyalanine encoding repeat in the 5' region of the Hoxd13 gene. We performed a detailed phenotypic and functional analysis of SPDH/SPDH embryos using skeletal preparations, histology, in situ hybridization, BrdU labeling of proliferating cells, and in vitro expression studies. The absence of normal phalangeal joints and the misexpression of genes involved in joint formation demonstrate a role for Hox-genes in joint patterning. The SPDH mutation results in abnormal limb pattering, defective chondrocyte differentiation, and in a drastic reduction in proliferation. Abnormal chondrocyte differentiation and proliferation persisted after birth and correlated with the expression of the mutant Hoxd13 and other Hox-genes during late-embryonic and postnatal growth.
Structure of Pseudomonas aeruginosa spermidine dehydrogenase: a polyamine oxidase with a novel heme-binding fold
FEBS J 2022 Apr;289(7):1911-1928.PMID:34741591DOI:10.1111/febs.16264.
The opportunistic pathogen Pseudomonas aeruginosa can utilize polyamines (including putrescine, cadaverine, 4-aminobutyrate, spermidine, and spermine) as its sole source of carbon and nitrogen. Spermidine dehydrogenase (SPDH) is a component of one of the two polyamine utilization pathways identified in P. aeruginosa, but little is known about its structure and function. Here, we report the first crystal structure of SPDH from P. aeruginosa to 1.85 Å resolution. The resulting core structure confirms that SPDH belongs to the polyamine oxidase (PAO) family with flavin-binding and substrate-binding domains. A unique N-terminal extension wraps around the flavin-binding domain of SPDH and is required for heme binding, placing a heme cofactor in close proximity to the FAD cofactor. Structural and mutational analysis reveals that residues in the putative active site at the re side of the FAD isoalloxazine ring form part of the catalytic machinery. PaSpdH features an unusual active site and lacks the conserved lysine that forms part of a lysine-water-flavin N5 atom interaction in other PAO enzymes characterized to date. Mutational analysis further confirms that heme is required for catalytic activity. This work provides an important starting point for understanding the role of SPDH, which occurs universally in P. aeruginosa strains, in polyamine metabolism.
Compressive phase object classification using single-pixel digital holography
Opt Express 2022 Jul 18;30(15):28057-28066.PMID:36236962DOI:10.1364/OE.463395.
A single-pixel camera (SPC) is a computational imaging system that obtains compressed signals of a target scene using a single-pixel detector. The compressed signals can be directly used for image classification, thereby bypassing image reconstruction, which is computationally intensive and requires a high measurement rate. Here, we extend this direct inference to phase object classification using single-pixel digital holography (SPDH). Our method obtains compressed measurements of target complex amplitudes using SPDH and trains a classifier using those measurements for phase object classification. Furthermore, we present a joint optimization of the sampling patterns used in SPDH and a classifier to improve classification accuracy. The proposed method successfully classified phase object images of handwritten digits from the MNIST database, which is challenging for SPCs that can only capture intensity images.
The mouse Hoxd13(SPDH) mutation, a polyalanine expansion similar to human type II synpolydactyly (SPD), disrupts the function but not the expression of other Hoxd genes
Dev Biol 2001 Sep 15;237(2):345-53.PMID:11543619DOI:10.1006/dbio.2001.0382.
Polyalanine expansion in the human HOXD13 gene induces synpolydactyly (SPD), an inherited congenital limb malformation. A mouse model was isolated, which showed a spontaneous alanine expansion due to a 21-bp duplication at the corresponding place in the mouse gene. This mutation (synpolydactyly homolog, SPDH), when homozygous, causes malformations in mice similar to those seen in affected human patients. We have studied the genetics of this condition, by using several engineered Hoxd alleles, as well as by looking at the expression of Hox and other marker genes. We show that the mutated SPDH protein induces a gain-of-function phenotype, likely by behaving as a dominant negative over other Hox genes. The mutation, however, seems to act independently from Hoxa13 and doesn't appear to affect Hox gene expression, except for a slight reduction of the HOXD13 protein itself. Developmental studies indicate that the morphological effect is mostly due to a severe retardation in the growth and ossification of the bony elements, in agreement with a general impairment in the function of posterior Hoxd genes.
Homeobox genes d11-d13 and a13 control mouse autopod cortical bone and joint formation
J Clin Invest 2010 Jun;120(6):1994-2004.PMID:20458143DOI:10.1172/JCI41554.
The molecular mechanisms that govern bone and joint formation are complex, involving an integrated network of signaling pathways and gene regulators. We investigated the role of Hox genes, which are known to specify individual segments of the skeleton, in the formation of autopod limb bones (i.e., the hands and feet) using the mouse mutant synpolydactyly homolog (SPDH), which encodes a polyalanine expansion in Hoxd13. We found that no cortical bone was formed in the autopod in SPDH/SPDH mice; instead, these bones underwent trabecular ossification after birth. SPDH/SPDH metacarpals acquired an ovoid shape and developed ectopic joints, indicating a loss of long bone characteristics and thus a transformation of metacarpals into carpal bones. The perichondrium of SPDH/SPDH mice showed abnormal morphology and decreased expression of Runt-related transcription factor 2 (Runx2), which was identified as a direct Hoxd13 transcriptional target. Hoxd11-/-Hoxd12-/-Hoxd13-/- triple-knockout mice and Hoxd13-/-Hoxa13+/- mice exhibited similar but less severe defects, suggesting that these Hox genes have similar and complementary functions and that the SPDH allele acts as a dominant negative. This effect was shown to be due to sequestration of other polyalanine-containing transcription factors by the mutant Hoxd13 in the cytoplasm, leading to their degradation. These data indicate that Hox genes not only regulate patterning but also directly influence bone formation and the ossification pattern of bones, in part via Runx2.