- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-189
Synonyms
Beta-2-glycoprotein 1, APC inhibitor, Activated protein C-binding protein, Anticardiolipin cofactor, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH, B2G1, BG, B2GP1.
Description
APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (20-345 a.a.) and having a molecular mass of 38.6kDa.
APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile filtered colorless solution.
Formulation
APOH protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Safety Data Sheet
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSGRTCPKP DDLPFSTVVP LKTFYEPGEE ITYSCKPGYV SRGGMRKFIC PLTGLWPINT LKCTPRVCPF AGILENGAVR YTTFEYPNTI SFSCNTGFYL NGADSAKCTE EGKWSPELPV CAPIICPPPS IPTFATLRVY KPSAGNNSLY RDTAVFECLP QHAMFGNDTI TCTTHGNWTK LPECREVKCP FPSRPDNGFV NYPAKPTLYY KDKATFGCHD GYSLDGPEEI ECTKLGNWSA MPSCKASCKV PVKKATVVYQ GERVKIQEKF KNGMLHGDKV SFFCKNKEKK CSYTEDAQCI DGTIEVPKCF KEHSSLAFWK TDASDVKPC.
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Background
Apolipoprotein-H Human Recombinant: Unleashing the Potential for Cardiovascular Health
Abstract:
Apolipoprotein-H (Apo-H) is a remarkable protein with diverse functions in lipid metabolism and thrombotic regulation. This research paper provides an in-depth analysis of Apo-H human recombinant, exploring its physiological roles, genetic implications, and potential therapeutic applications. Understanding the intricacies of Apo-H sheds light on its significance in cardiovascular health and highlights its potential as a therapeutic target. This article offers a concise yet comprehensive examination of Apo-H, emphasizing its impact on human well-being.
Introduction:
Cardiovascular health is of utmost importance in preventing and managing cardiovascular diseases. Apo-H, a multifunctional protein involved in lipid metabolism and thrombotic regulation, offers a unique perspective in understanding these processes. This paper explores the multifaceted nature of Apo-H, elucidating its genetic implications and its role as a potential guardian of cardiovascular well-being.
Structure and Function of Apolipoprotein-H:
Apo-H possesses a complex molecular structure, consisting of distinct domains that facilitate interactions with lipoproteins and coagulation factors. It plays a critical role in lipid transport, regulating triglyceride-rich lipoproteins. Additionally, Apo-H contributes to the delicate balance of thrombotic processes through its anticoagulant and fibrinolytic activities.
Genetic Implications of Apolipoprotein-H:
The APOH gene, responsible for encoding Apo-H, exhibits genetic variations that can influence an individual's susceptibility to cardiovascular diseases. Understanding these genetic variations helps identify potential risk factors and therapeutic targets for cardiovascular disorders.
Apolipoprotein-H and Cardiovascular Diseases:
Apo-H has garnered significant attention in the field of cardiovascular diseases, particularly in relation to atherosclerosis and thrombotic events. Its versatility allows modulation of inflammatory responses, maintenance of endothelial function, and regulation of coagulation pathways. Investigating the intricate interplay between Apo-H and cardiovascular processes may yield innovative therapeutic strategies.
Production of Apolipoprotein-H Human Recombinant:
Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, enable the production of Apo-H human recombinant. These methods facilitate large-scale production, purification, and characterization of Apo-H, providing opportunities for potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-H Human Recombinant:
Leveraging the therapeutic potential of Apo-H holds promise in cardiovascular interventions. Strategies aimed at enhancing Apo-H expression or function may contribute to lipid homeostasis, prevent thrombotic events, and reduce the risk of cardiovascular diseases.
Conclusion:
Apolipoprotein-H human recombinant represents a fascinating area of research, bridging the realms of lipid metabolism and cardiovascular health. Understanding the genetic implications and cardiovascular protective properties of Apo-H is pivotal in advancing our knowledge and developing novel therapeutic approaches for cardiovascular diseases. Continued investigation into the functions and mechanisms of Apo-H will likely unveil innovative strategies for promoting cardiovascular well-being.