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AB98085

Recombinant Human RHOC protein

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(1 Publication)

Recombinant Human RHOC protein is a Human Full Length protein, in the 1 to 190 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ARH9, ARHC, RHOC, Rho-related GTP-binding protein RhoC, Rho cDNA clone 9, h9

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SDS-PAGE - Recombinant Human RHOC protein (AB98085)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human RHOC protein (AB98085)

15% SDS-PAGE analysis of 3μg ab98085

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P08134

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGC","proteinLength":"Full Length","predictedMolecularWeight":"23.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":190,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P08134","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RHOC also known as ras homolog family member C is a small GTPase with a molecular mass of approximately 22 kDa. This protein part of the Rho family is involved in various cellular functions including motility and mitosis. RHOC is widely expressed in different tissues but shows higher levels in certain tumor cells. Through its role in actin cytoskeleton organization RHOC mediates cellular structure and activity by binding to GDP and GTP molecules thereby controlling cell morphology and movement.
Biological function summary

RHOC influences cell migration invasion and proliferation key processes in cancer progression. It functions within the Rho family of GTPases interacting with other proteins like ROCK and mDia to regulate cytoskeletal dynamics. RHOC does not operate alone; it works as part of signaling complexes that affect cellular mechanisms such as adhesion and vesicle trafficking. Its activity modulates the balance between cell stability and movement making it significant in tissue remodeling and repair.

Pathways

RHOC plays pivotal roles in the Rho/ROCK and PI3K/Akt signaling pathways. Through these pathways it interacts with related GTPases like RHOA and RAC1. In the Rho/ROCK pathway RHOC influences actin cytoskeleton rearrangement impacting cell contractility and motility. Via the PI3K/Akt pathway RHOC is linked to cell survival and growth involving other proteins like PTEN and mTOR highlighting its function in integrating external signals for cellular response.

RHOC is relevant in cancer and cardiovascular diseases. In cancer elevated RHOC expression correlates with increased invasiveness and metastasis particularly in breast and pancreatic cancers. This association involves proteins such as integrins and cadherins which aid in cell adhesion and migration. RHOC is also implicated in cardiovascular disorders where abnormal cell migration and proliferation contribute to atherosclerosis. Understanding these interactions assists in potential targeting of RHOC for therapeutic purposes.
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Specifications

Form

Liquid

Additional notes

ab98085 was purified using conventional chromatography techniques.

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General info

Function

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Post-translational modifications

(Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly.. (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:24905543).

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Product protocols

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Target data

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.
See full target information RHOC
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 35:e21627 PubMed33948992

2021

Tumor necrosis factor-induced ArhGEF10 selectively activates RhoB contributing to human microvascular endothelial cell tight junction disruption.

Applications

Unspecified application

Species

Unspecified reactive species

Alamzeb Khan,Weiming Ni,Francesc Lopez-Giraldez,Martin S Kluger,Jordan S Pober,Richard W Pierce
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