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FITC标记的去整合素样金属蛋白酶32抗体

2017-5-3


                                   FITC标记的去整合素样金属蛋白酶32抗体                                                                                                                                                
英文名称Anti-ADAM32/FITC
中文名称:FITC标记的去整合素样金属蛋白酶32抗体
别    名A disintegrin and metalloproteinase domain 32; ADA32_HUMAN; ADAM 32; Adam32; Disintegrin and metalloproteinase domain-containing protein 32.   

详细介绍:


规格:100ul 
说 明 书100ul  
研究领域肿瘤  细胞生物  免疫学  信号转导  激酶和磷酸酶  细胞骨架  细胞外基质  泛素  
抗体来源Rabbit
克隆类型Polyclonal
交叉反应 Human, Mouse, Rat, Dog, Cow, Horse, Guinea Pig, 
产品应用IF=1:50-200  
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量68kDa
细胞定位细胞膜 
性    状Lyophilized or Liquid
浓    度1mg/ml
免 疫 原KLH conjugated synthetic peptide derived from human ADAM32
亚    型IgG
纯化方法affinity purified by Protein A
储 存 液0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存条件Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.

相关资料:


产品介绍background:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

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