Anti-ERp29抗体This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum （ER）.

产品编号 yb-5121R
英文名称 Anti-ERp29抗体
中文名称 内质网蛋白29抗体
别    名 Chromosome 12 open reading frame 8; Endoplasmic reticulum lumenal protein ERp28; Endoplasmic reticulum protein 29; Endoplasmic reticulum protein 29 isoform 1; Endoplasmic reticulum protein ERp29; ERp28; ERp31; PDI-DB; C12orf8.
Anti-ERp29抗体   
说 明 书 0.1ml  0.2ml  
研究领域 肿瘤  细胞生物  免疫学  转录调节因子  
抗体来源 Rabbit
克隆类型 Polyclonal
交叉反应 Human, Mouse, Rat, Dog, Pig, Cow, Sheep, 
产品应用 WB=1:100-500 ELISA=1:500-1000 IHC-P=1:100-500 IHC-F=1:100-500 IF=1:100-500 （石蜡切片需做抗原修复） 
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量 26kDa
细胞定位 细胞浆 
性    状 Lyophilized or Liquid
浓    度 1mg/1ml
免 疫 原 KLH conjugated synthetic peptide derived from human ERp29
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
PubMed PubMed
产品介绍 background:
This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].

Function:
Proper protein folding and post-translational modifications are essential for secretory protein export out of the endoplasmic reticulum. This task is accomplished by chaperone proteins such as protein disulfide isomerase (PDI), GRP94, and BiP. A recently characterized protein, designated ERp29, is closely related to these chaperone proteins and appears to be upregulated during ER stress conditions. ERp29 is a soluble 259-residue protein that is localized to the lumen of the endoplasmic reticulum in all mammalian cells. Research has shown that there are two primary domains within ERp29. The first is the C-terminal region that is a novel, all helical, fold that is most likely involved with ERp29 retention to the ER. The second is the N-terminal region that resembles that of PDI’s thioredoxin module. The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER.

Subcellular Location:
Endoplasmic reticulum