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Rabbit Anti-p27 Polyclonal Antibody#abs135610

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Description

Catalog-specification	Delivery time	USD price
abs135610-100ug	1-2 Weeks	301.0
abs135610-50ug	1-2 Weeks	201.0

Overview
catalog	abs135610
Description	p27 Kip1, a member of the Cip/Kip family of cyclin-dependent kinase inhibitors, exerts its role in controlling the G1 restriction point through inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes, much like its counterparts p57 Kip2 and p21 Waf1/Cip1. Naturally, levels of p27 increase in quiescent cells and in cells treated with cAMP or other negative regulators of the cell cycle. However, the downregulation of p27 can be induced through various means, such as treatment with interleukin 2 or other mitogens. In these cases, phosphorylation of p27 occurs, leading to its degradation via the ubiquitin-proteasome pathway (1-4).
Other names	Cyclin-dependent kinase inhibitor 1B, also known as CDKN1B or p27Kip1, is a vital protein that helps in regulating the cell cycle. It is coded by the CDKI1B gene, and its primary function is to inhibit the progression of the cell cycle from the G1 phase to the S phase. CDKN1B acts by binding to and inhibiting the activity of cyclin-dependent kinases (CDKs), which are responsible for promoting cell cycle progression. CDKN1B is a tumor suppressor protein that is frequently down-regulated in cancer cells. By inhibiting CDK activity, p27Kip1 prevents uncontrolled cell proliferation and promotes the differentiation of cells into specialized tissues. Linke many other tumor suppressors, CDKN1B's expression can be affected by environmental stimuli such as DNA damage and exposure to chemicals. Low levels of CDKN1B expression have been linked to a higher risk of cancer development. In summary, CDKN1B is an important component of the cellular machinery that controls cell division. Its role as a regulator of the cell cycle places it at the center of many signaling pathways, making it a crucial player in cancer biology.
Source	Rabbit
Specificity	The primary purpose of the p27 Antibody is to identify and measure the levels of total p27 protein present in an organism without any external interference. To accomplish this, the p27 Antibody specifically binds to the endogenous form of p27 protein in order to accurately analyze its expression levels. By utilizing this antibody, researchers can obtain reliable data regarding the abundance and distribution of p27 protein within biological samples.
Species Reactivity	Human;Mouse;Rat
Antigen	p27
Application	The dilution ratios for western blot (WB) range from 1:200 to 1:500. For immunohistochemistry (IHC), the dilution ratios are 1:50 to 1:200. As for immunofluorescence/immunocytochemistry (IF/ICC), the recommended dilutions vary from 1:100 to 1:500. For ELISA using peptide, the dilution range is 1:20000 to 1:40000. Please note that the generated content is rearranged in order to present the same information but in a different format.
Immunogen	Fusion protein of human p27.
MW	27kDa
Properties
Concentration	1mg/ml
purification	The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin .
Clonality	Polyclonal Antibody
Stability & Storage	Store at -20 °C for one year. Avoid repeated freeze/thaw cycles
Storage buffer	Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
Target
Background	Important regulator of cell cycle progression. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.
Tissue specificity	Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.
Posttranslational modification	Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G0-G1 phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, cMYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF.Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation.Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation (By similarity).
Celluar localization	Cytosol;Endosome;Nucleus;
UniPort	P46527