P0078
Anti-PMP22 antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-GAS3, Anti-Growth arrest-specific 3, Anti-Peripheral myelin protein 22
产品名称
Anti-PMP22 antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~22 kDa
species reactivity
human
concentration
~1.0 mg/mL
technique(s)
immunohistochemistry: 2.5-5 μg/mL using biotin/ExtrAvidin™-Peroxidase staining of formalin-fixed, paraffin-embedded human spinal cord sections
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PMP22(5376)
mouse ... Pmp22(18858)
rat ... Pmp22(24660)
Biochem/physiol Actions
Anti-PMP22 recognizes human PMP22.
PMP22 (peripheral myelin protein-22) participates in the progression of CNS (central nervous system) myelin. It modulates self-renewal and chemoresistance of gastric cancer cells. Mutation in PMP22 results in Charcot-Marie tooth disease.
PMP22 plays a role in peripheral nerve myelin formation, cell-cell interactions, and cell proliferation. Overexpression of PMP22 is implicated in the neoplastic transformation of normal tissue to pre-malignant lesions and cancer of the pancreas and osteoblasts.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
PMP22 (peripheral myelin protein-22) is a tetraspan integral membrane protein, that contains four putative transmembrane domains. It is expressed in the peripheral nervous system. PMP22 is produced by myelinating Schwann cells. It is an important constituent of peripheral myelin. This gene is mapped to human chromosome 17p11.2.
Immunogen
synthetic peptide corresponding to amino acid residues 118-133 of human PMP22, with an added cysteine, conjugated to KLH. The corresponding sequence differs by 3 amino acids in rat and mouse.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
Legal Information
BiotinTag is a trademark of Sigma-Aldrich Co. LLC
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Maaike van Dartel et al.
Cancer genetics and cytogenetics, 152(2), 113-118 (2004-07-21)
The peripheral myelin protein (PMP22) gene is highly expressed in peripheral Schwann cells and encodes an important constituent of the myelin sheath. It is also expressed at lower levels in other normal tissues in which the protein is supposed to
Shazia Irshad et al.
Science translational medicine, 5(202), 202ra122-202ra122 (2013-09-13)
Many newly diagnosed prostate cancers present as low Gleason score tumors that require no treatment intervention. Distinguishing the many indolent tumors from the minority of lethal ones remains a major clinical challenge. We now show that low Gleason score prostate
A novel missense mutation in peripheral myelin protein-22 causes Charcot-Marie-Tooth disease
Li, Li-Xi and Dong
Chinese Medical Journal (English Edition), 130(15), 1779-1779 (2017)
PMP22 regulates self-renewal and chemoresistance of gastric cancer cells
Cai W, et al.
Molecular Cancer Therapeutics, molcanther-molcan0750 (2017)
G Jackson Snipes et al.
Annals of the New York Academy of Sciences, 883(1), 143-151 (1999-10-01)
The gain of function phenotypes exhibited by the heterozygous Tr, Tr-J, and CMT1A mutations indicate that these mutations interfere with more than the function of a single PMP22 allele. The identification of proteins that interact with PMP22 and that are
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