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Search results

1000 results found for “aprotinin”

Name

Description

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  • View Data Sheet

    Name :

    GDI2 Human

    Description:

    GDP Dissociation Inhibitor 2 Human Recombinant

    GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    Product # :

    PRO-1948

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    Quantity :

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    Description

    GDI2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (1-445) and having a molecular mass of 53.1 kDa.GDI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

    • Synonyms

      GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESASIT PLEDLYKRFK IPGSPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVTEG SFVYKGGKIY KVPSTEAEAL ASSLMGLFEK RRFRKFLVYV ANFDEKDPRT FEGIDPKKTT MRDVYKKFDL GQDVIDFTGH ALALYRTDDY LDQPCYETIN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPIEE IIVQNGKVIG VKSEGEIARC KQLICDPSYV KDRVEKVGQV IRVICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SFAHNVAAQG KYIAIVSTTV ETKEPEKEIR PALELLEPIE QKFVSISDLL VPKDLGTESQ IFISRTYDAT THFETTCDDI KNIYKRMTGS EFDFEEMKRK KNDIYGED.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gdi2 Human
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

    Price :

    Quantity :

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    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Ta Human
  • View Data Sheet

    Name :

    PRSS28 Mouse

    Description:

    Protease Serine 28 Mouse Recombinant

    Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.

    Product # :

    ENZ-987

    Price :

    Quantity :

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    • More Info

    Description

    PRSS28 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (27-274a.a.) and having a molecular mass of 28.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PRSS28 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PRSS28 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine protease 28, also known as Prss28, is a member of the S1 serine proteinase family with a conserved Histidine-Aspartic Acid-Serine catalytic triad. Prss28 shows mixed substrate specificity which silences signaling through proteinase-activated receptors. Furthermore, Prss28 is involved with embryo hatching and its activity is vital for successful implantation.

    • Synonyms

      Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      KPVGIVGGQC TPPGKWPWQV SLRMYSYEVN SWVHICGGSI IHPQWILTAA HCIQSQDADP AVYRVQVGEV YLYKEQELLN ISRIIIHPDY NDVSKRFDLA LMQLTALLVT STNVSPVSLP KDSSTFDSTD QCWLVGWGNL LQRVPLQPPY QLHEVKIPIQ DNKSCKRAYR KKSSDEHKAV AIFDDMLCAG TSGRGPCFGD SGGPLVCWKS NKWIQVGVVS KGIDCSNNLP SIFSRVQSSL AWIHQHIQLE HHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Prss28 Mouse
  • View Data Sheet

    Name :

    GP1BB Human

    Description:

    Glycoprotein Ib Platelet Subunit Beta Human Recombinant

    GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.

    Product # :

    PRO-2774

    Price :

    Quantity :

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    • More Info

    Description

    GP1BB Human Recombinant is a single, glycosylated, polypeptide chain (26-147 a.a) containing a total of 131 amino acids, having a molecular mass of 14.0 kDa. GP1BB is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The GP1BB solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      GPIBB, glycoprotein Ib platelet subunit beta, BDPLT1,GP-Ib beta, BS, CD42C ,GPIbbeta, Antigen CD42b-beta, GPIb-beta, GPIbB, Platelet glycoprotein Ib beta chain.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      DGSCPAPCSC AGTLVDCGRR GLTWASLPTA FPVDTTELVL TGNNLTALPP GLLDALPALR TAHLGANPWR CDCRLVPLRA WLAGRPERAP YRDLRCVAPP ALRGRLLPYL AEDELRAACA PGPLCHHHHH H.

    • Background

      Glycoprotein 1b beta (GP1BB) is a crucial component of the platelet glycoprotein Ib-IX-V complex, playing a pivotal role in platelet function and hemostasis. This research aims to explore the structure, function, and implications of GP1BB protein in platelet adhesion, aggregation, and the development of thrombotic disorders. Understanding the molecular mechanisms and regulatory roles of GP1BB can provide valuable insights into its potential as a therapeutic target for thrombotic diseases.

      Structure and Expression of GP1BB Protein:

      GP1BB is a transmembrane protein consisting of an extracellular domain, a single transmembrane region, and a short cytoplasmic tail. It is predominantly expressed on the surface of platelets, where it interacts with von Willebrand factor (VWF) and other components of the glycoprotein Ib-IX-V complex. GP1BB is crucial for mediating platelet adhesion to damaged endothelium and the formation of stable platelet aggregates at the site of injury.

      GP1BB and Platelet Adhesion:

      GP1BB interacts with VWF, which is exposed upon vascular injury. This interaction facilitates the initial attachment of platelets to the damaged endothelium. GP1BB also participates in the formation of high-affinity bonds between platelets and VWF, contributing to the stabilization of platelet adhesion and the initiation of platelet aggregation. Dysregulation of GP1BB-mediated platelet adhesion can lead to abnormal clot formation and thrombotic disorders.

      Implications of GP1BB in Thrombotic Disorders:

      Defects or mutations in the GP1BB gene can result in Bernard-Soulier syndrome (BSS), a rare inherited bleeding disorder characterized by giant platelets, thrombocytopenia, and impaired platelet adhesion. BSS patients often experience excessive bleeding and bruising due to defective GP1BB function. On the other hand, abnormal activation or overexpression of GP1BB has been associated with increased risk of thrombotic events, such as myocardial infarction and stroke.

      Therapeutic Strategies Targeting GP1BB:

      Given its crucial role in platelet function and thrombotic disorders, GP1BB represents a potential target for therapeutic interventions. Strategies aimed at modulating GP1BB expression or function have been explored. This includes the development of monoclonal antibodies or small molecule inhibitors that selectively target GP1BB and interfere with its interaction with VWF or other binding partners. Such approaches aim to prevent excessive platelet adhesion and aggregation, reducing the risk of thrombotic events.

      Challenges and Future Directions:

      While targeting GP1BB shows promise, several challenges need to be addressed. The development of specific inhibitors or modulators of GP1BB that do not interfere with its physiological functions is crucial. Additionally, understanding the complex interplay between GP1BB and other platelet receptors and signaling pathways is essential for the development of effective therapeutic strategies.

      Conclusion:

      The study of GP1BB protein provides valuable insights into its central role in platelet adhesion, aggregation, and thrombotic disorders. Understanding the molecular mechanisms and functional implications of GP1BB opens avenues for the development of targeted therapies for thrombotic diseases. Further research on GP1BB protein, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to mitigate the risk of thrombotic events and improve patient outcomes.

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    Gp1Bb Human
  • View Data Sheet

    Name :

    REN Human, sf9

    Description:

    Renin Human Recombinant, sf9

    REN, HNFJ2, Renin, Angiotensinogenase.

    Product # :

    PRO-2342

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    Description

    REN Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (24-406) and having a molecular mass of 43.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).REN is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    REN protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

    • Synonyms

      REN, HNFJ2, Renin, Angiotensinogenase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Amino Acid Sequence

      LPTDTTTFKR IFLKRMPSIR ESLKERGVDM ARLGPEWSQP MKRLTLGNTT SSVILTNYMD TQYYGEIGIG TPPQTFKVVF DTGSSNVWVP SSKCSRLYTA CVYHKLFDAS DSSSYKHNGT ELTLRYSTGT VSGFLSQDII TVGGITVTQM FGEVTEMPAL PFMLAEFDGV VGMGFIEQAI GRVTPIFDNI ISQGVLKEDV FSFYYNRDSE NSQSLGGQIV LGGSDPQHYE GNFHYINLIK TGVWQIQMKG VSVGSSTLLC EDGCLALVDT GASYISGSTS SIEKLMEALG AKKRLFDYVV KCNEGPTLPD ISFHLGGKEY TLTSADYVFQ ESYSSKKLCT LAIHAMDIPP PTGPTWALGA TFIRKFYTEF DRRNNRIGFA LARLEHHHHH H.

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    Ren Human Sf9
  • View Data Sheet

    Name :

    REN Mouse

    Description:

    Renin Mouse Recombinant

    Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.

    Product # :

    PRO-2251

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    Description

    REN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 387 amino acids (22-402 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).REN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    REN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

    • Synonyms

      Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      LPTRTATFER IPLKKMPSVR EILEERGVDM TRLSAEWGVF TKRPSLTNLT SPVVLTNYLN TQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA CGIHSLYESS DSSSYMENGS DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI PFMLAKFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEEV FSVYYNRGSH LLGGEVVLGG SDPQHYQGNF HYVSISKTDS WQITMKGVSV GSSTLLCEEG CAVVVDTGSS FISAPTSSLK LIMQALGAKE KRIEEYVVNC SQVPTLPDIS FDLGGRAYTL SSTDYVLQYP NRRDKLCTLA LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA RHHHHHH.

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    Ren Mouse
  • View Data Sheet

    Name :

    HIV-1 NEF Biotin

    Description:

    HIV-1 nef Recombinant Biotin Labeled

    Product # :

    HIV-009

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    Description

    Recombinant HIV-1 nef Biotin Labeled is a full length protein produced in E.coli and having a molecular mass of 27kDa. HIV-1 nef Biotin is purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    HIV-1 nef Biotin protein solution containing PBS & 0.05%(v/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIV-1 Nef is anessential factor for efficient viral replication and pathogenesis and therefore is produced shortly after virus infection. HIV-1 Nef is also facilitates virus replication and enhances virions infectivity. Nef exerts pleiotropic effects: decreases cell surface CD4 antigen by interacting with the Src family kinase LCK, down-modulates surface MHC-I molecules and protects the infected cell from apoptosis in order to keep it alive until the next virus generation is mature. Nef protein bypasses host T-cell signaling byinducing a trascriptional program almost identical to that of anti-CD3 cell activation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      HIV-1 nef Biotin although stable at 4°C for 1 week, should be stored below -18°C.Please prevent freeze thaw cycles

    • Applications

      Western Blotting, SDS Page

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    Hiv 1 Nef
  • View Data Sheet

    Name :

    APOB Human

    Description:

    Apolipoprotein-B Human

    APOB, APO-B, Apolipoprotein B.

    Product # :

    CYT-1042

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    Description

    Human APOB produced from Human plasma having a molecular mass of 550 kDa.

    Source

    Human Plasma.

    Formulation

    The protein was lyophilized in a solution contains 50mM NaCl, 50mM Na₂co₃, PH 10 and deoxycholate.

    Purity

    Greater than 90.0%.

    More Info

    • Introduction

      ApoB is the main apolipoprotein of LDL, IDL, VLDL and chylomicrons particles that serves as the carrier of lipids (fat molecules), as well as cholesterol, in the water surrounding the cells within every tissue across the body. Though all the functional aspects of Apolipoprotein B within the LDL and other elements are considered to be rather uncertain, it serves as the key organizing protein of all other carriers of lipids. across LDL membranes, apolipoprotein B also serves as a ligand for LDL receptors in many cells across the body, meaning, it shows that lipid carriers that are set to cross into cells with Apolipoprotein B receptors, this is the way that lipids are transported within and into cells.

    • Synonyms

      APOB, APO-B, Apolipoprotein B.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized APOB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution, APOB should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized APOB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Starting material donor has been tested and certified negative for antibodies to HIV-1,
      HIV-2, HCV, HBSAG, HBc.

    • Background

      Apolipoprotein-B Human: Unveiling the Key Player in Cholesterol Transport

      Abstract:

      Apolipoprotein-B (ApoB), a pivotal component of lipoproteins, plays a critical role in cholesterol metabolism and transportation. It is primarily synthesized in the liver and intestines, existing in two main isoforms: ApoB-100 and ApoB-48. This research paper aims to provide a comprehensive overview of ApoB human, emphasizing its physiological functions, regulatory mechanisms, and implications in cardiovascular diseases. By delving into the intricacies of ApoB, we can gain valuable insights into its significance as a therapeutic target and potential biomarker.

      Introduction:

      The prevalence of cardiovascular diseases necessitates a deeper understanding of the mechanisms governing cholesterol metabolism. ApoB, an integral component of lipoproteins, holds the key to unlocking vital insights into cholesterol transport and its association with atherosclerosis.

      Structure and Function of Apolipoprotein-B:

      ApoB exhibits a complex molecular structure, consisting of functional domains that enable its interaction with lipids and receptors. ApoB-100, the longer isoform, is primarily associated with low-density lipoprotein (LDL) particles, while ApoB-48 is present in chylomicrons and chylomicron remnants. These isoforms serve distinct roles in lipoprotein metabolism and cholesterol delivery to peripheral tissues.

      Regulation of Apolipoprotein-B:

      The synthesis and secretion of ApoB are tightly regulated processes influenced by various factors, including dietary and genetic factors. Transcriptional and post-transcriptional mechanisms govern the expression and processing of ApoB, ensuring its proper function in cholesterol transport.

      Apolipoprotein-B and Cardiovascular Diseases:

      Elevated levels of ApoB-containing lipoproteins, such as LDL, have been implicated in the development of atherosclerosis and cardiovascular diseases. The ratio of ApoB to ApoA-I, known as the ApoB/ApoA-I ratio, serves as a reliable marker for cardiovascular risk assessment, with higher ratios indicating increased risk.

      Therapeutic Implications of Apolipoprotein-B:

      Targeting ApoB presents a promising avenue for managing dyslipidemia and reducing cardiovascular risk. Strategies aimed at reducing ApoB production or enhancing its clearance have shown efficacy in clinical trials, underscoring the potential of ApoB as a therapeutic target.

      Conclusion:

      Apolipoprotein-B human serves as a cornerstone in cholesterol transport, playing a crucial role in lipoprotein metabolism and its implications for cardiovascular health. By unraveling the intricate interplay between ApoB, cholesterol metabolism, and atherosclerosis, we can pave the way for novel therapeutic interventions and improved risk assessment in cardiovascular diseases.

      What is the molecular weight/Mw of APOB Protein?
      APOB Protein has a total Mw of 550kDa.

      What is the source or expression system of APOB Protein?
      Human Plasma.

      What is the Purity of APOB Protein?
      APOB Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOB Protein?
      The biological functionality of APOB Protein will be determined in the future.

      What applications can APOB Protein be used in?
      APOB Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOB Protein?
      The endotoxin level is minimal, APOB Protein was purified using conventional chromatography techniques.

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    Apolipoprotein B Human
  • View Data Sheet

    Name :

    ACTN1 Human

    Description:

    Actinin Alpha 1 Human Recombinant

    ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    Product # :

    PRO-2227

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    Description

    ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.

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    Actn1 Human
  • View Data Sheet

    Name :

    CTRB1 Human

    Description:

    Chymotrypsinogen-B1, Human Recombinant

    Product # :

    ENZ-1016

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    Description

    Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.

    Source

    E.coli

    Formulation

    The Human CTRB1 was lyophilized without any additives.

    Purity

    Greater than 95% as determined by HPLC.

    Biological Activity

    1100 units/mg protein.
    One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.

    More Info

    • Introduction

      Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.

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    Ctrb1 Human
  • View Data Sheet

    Name :

    KRT14 Human

    Description:

    Cytokeratin 14 Human Recombinant

    Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    Product # :

    PRO-348

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    Description

    Cytokeratin 14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 51,530 Dalton. The KRT14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.

    • Synonyms

      Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT14 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CK-14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCI, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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    Krt14 Human
  • View Data Sheet

    Name :

    KRT19 Human

    Description:

    Cytokeratin 19 Human Recombinant

    Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    Product # :

    PRO-350

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    Description

    Cytokeratin 19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 44,098 Dalton. The KRT19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.

    • Synonyms

      Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT19 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized KRT19 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCl, 2 mM dithiothreitol, 10 mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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    Krt19 Human
  • View Data Sheet

    Name :

    Cathepsin H Antibody

    Description:

    Cathepsin H, Mouse Anti Human

    Cathepsin H, CTSH, CPSB, ACC-4, ACC-5, MGC1519, minichain, DKFZp686B24257.

    Product # :

    ANT-405

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      Cathepsin H is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. Cathepsin H is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. Cathepsin H, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of the Cathepsin H gene has been associated with malignant progression of prostate tumors.

    • Synonyms

      Cathepsin H, CTSH, CPSB, ACC-4, ACC-5, MGC1519, minichain, DKFZp686B24257.

    • Immunogen

      Anti-human Cathepsin H mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cathepsin H amino acids 23-335 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and κ light chain.

    • Clone

      P3G8AT.

    • Applications

      Cathepsin H antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Cathepsin H antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Cathepsin H Antibody
  • View Data Sheet

    Name :

    ACTH

    Description:

    Adrenocorticotropic Hormone

    Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    Product # :

    HOR-279

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    Description

    The Molecular formula of Adrenocorticotropic Hormone is C136H210N40O31S and the molecular weight is 2933.5 Dalton.

    Formulation

    The ACTH hormone was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Adrenocorticotropic hormone, as its name implies, stimulates the adrenal cortex. More specifically, it stimulates secretion of glucocorticoids such as cortisol, and has little control over secretion of aldosterone, the other major steroid hormone from the adrenal cortex. Stimulates secretion of adrenal corticosteroids and induces growth of adrenal cortex. ACTH also called Tetracosactide directly activates G-proteins. A stimulator of adenylate cyclase and cAMP formation.

    • Synonyms

      Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Adrenocorticotropic Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACTH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ACTH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Acth
  • View Data Sheet

    Name :

    LGALS8 Human, His

    Description:

    Galectin-8 Human Recombinant, His Tag

    Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    Product # :

    CYT-727

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    • SDS-PAGE

    Description

    LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.

    SDS-PAGE

    LGALS8 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

    • Synonyms

      Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

    • Background

      What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.

      What is the source or expression system of LGALS8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
      The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
      sequence of LGALS8 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

      What applications can LGALS8 HUMAN, HIS Protein be used in?
      LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS8 HUMAN, HIS Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Lgals8 Human His
  • View Data Sheet

    Name :

    C3 Human

    Description:

    Complement C3 Human

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2684

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    Description

    Human Complement C3 produced in Human plasma having a molecular mass of 185 kDa.

    Source

    Human Plasma.

    Formulation

    C3 solution contains phosphate buffer saline.

    Purity

    Greater than 94.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Native human C3 is a naturally glycosylated polypeptide containing two disulfide-linked chains. C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      C3 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1,HIV-2, HCV, HTLV-I &II, STS and HBSAG.

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    C3 Human
  • View Data Sheet

    Name :

    C7 Human

    Description:

    Complement C7 Human

    Complement component C7, C7.

    Product # :

    PRO-2694

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    Description

    Human Complement C7 produced in Human plasma having a molecular mass of 92.4kDa.

    Source

    Human Plasma.

    Formulation

    C7 protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C7 is necessary for formation of the membrane attack complex and is activated by bindingat the cell membrane to recently-formed C5b,C6 complexes. Each pathway of complement activation generates proteolytic enzyme complexes which bind the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing C5a and activating C5b. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC. The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell.

    • Synonyms

      Complement component C7, C7.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C7 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    C7 Human
  • View Data Sheet

    Name :

    Thrombin Human, HEK

    Description:

    Thrombin Human Recombinant, HEK

    Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.

    Product # :

    PRO-1422

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    Description

    Recombinant Human Thrombin produced in HEK cells, having a total molecular weight of 36kDa. The Thrombin is purified by proprietary chromatographic techniques.

    Source

    HEK

    Formulation

    The Thrombin solution contains 20mM MES, pH6.0 and 500mM Choline Chloride.

    Biological Activity

    5396 NIH Units/mg.
    The activity was determined in NIH units by comparing to Sigma’s human plasma thrombin. Protein concentration was measured using E(0.1%)@280nm = 1.83.

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Synonyms

      Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store frozen at -20°C to -80°C for long periods of time. Avoid multiple freeze-thaw cycles.

    • Assay Conditions

      Thrombin (1nM) was assayed using SPECTROZYME TH as a substrate (20µM) in 5mM Tris-HCl (pH8.0), 0.1% PEG, 200mM NaCl at 25°C.

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    Thrombin Human Recombinant
  • View Data Sheet

    Name :

    TNNI3 Human Chimeric

    Description:

    Cardiac Troponin-I Chimeric Human Recombinant

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2790

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    Description

    TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.

    Source

    Escherichia Coli.

    Formulation

    TNNI3 was lyophilized in 50mM Tris-HCl, 5mM Calcium chloride, 0.7M KCl and 0.1% 2-mercaptoethanol, pH 7.5

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cardiac Troponin-I Chimeric although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TNNI3 in buffer containing BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin I (TNNI3) is a crucial regulatory protein in cardiac muscle, playing a central role in the regulation of muscle contraction. Understanding the structure and function of TNNI3 is essential for unraveling the complexities of cardiac muscle physiology and exploring therapeutic interventions for cardiac diseases. Chimeric TNNI3 proteins, which combine segments from different isoforms or species, offer a unique opportunity to investigate the role of specific regions in TNNI3 function and to potentially develop novel therapies. This research aims to provide a comprehensive exploration of chimeric TNNI3 proteins, elucidating their functions, structural significance, and potential applications in cardiology and biomedical research.

      The primary objective of this research is to elucidate the functional significance of chimeric TNNI3 proteins in cardiac muscle. In vitro and ex vivo experiments, utilizing engineered chimeric TNNI3 constructs and cardiac tissue models, will be conducted to investigate how these proteins influence muscle contractility, calcium sensitivity, and response to pathological conditions. Understanding these mechanisms is fundamental for deciphering the roles of specific TNNI3 regions in cardiac muscle function.

      The second objective is to assess the therapeutic potential of chimeric TNNI3 proteins in cardiac diseases. Experimental studies involving animal models and cellular systems will explore the use of chimeric TNNI3 proteins as potential therapeutic agents for heart conditions. These investigations may provide valuable insights into novel treatment strategies targeting cardiac muscle function.

      The third objective is to explore the broader applications of chimeric TNNI3 proteins in biotechnology and drug development. Research will investigate the use of chimeric TNNI3-expressing cells and tissues as models for studying cardiac disorders and for developing innovative approaches in regenerative medicine and pharmacology.

      By delving into the functions and roles of chimeric TNNI3 proteins, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology, biotechnology, and drug development

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tnni3 Chimeric
  • View Data Sheet

    Name :

    Soybean P34 GST

    Description:

    Soybean P34 Protein Recombinant, GST Tag

    Product # :

    ALR-005

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    Description

    The E.Coli derived GST Tag recombinant protein, 36kDa, contains Soybean P34 Protein epitopes 214-261, 351-379 amino acids.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-HCl, pH 8.0, 60mM NaCl, 10mM glutathione and 50% glycerol.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The P34 protein is the main allergen for soybean sensitive humans. Soybean protein P34, a thiol protease belonging to the papain family, is a monomeric allergen having an N-terminal amino acid sequence and amino acid composition identical to that of the seed 34kDa protein. It is an insoluble glycoprotein having a pI of 4.5 and a calculated mass of 28.643 Dalton, representing 2–3% of total soybean protein. Upon glycosylation, the mass will be somewhat larger, resulting in a ~32kDa band in non-reduced SDS PAGE gels. It exhibits no enzymatic function due to an absence of the catalytic cysteine. P34 is stored in storage vacuoles of soybean cotyledons.

    • Stability

      Soybean P34 His although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Purification Method

      Purified by proprietary chromatographic technique

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Soybean P34 His
  • View Data Sheet

    Name :

    ITAC (63-87) Human

    Description:

    ITAC (63-87 a.a.) Human Recombinant

    ITAC, I-TAC, CXCL-11, CXCL11.

    Product # :

    CHM-049

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    Description

    The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      ITAC, I-TAC, CXCL-11, CXCL11.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized I-TAC at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.

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    Cxcl11 Human
  • View Data Sheet

    Name :

    Activin B Human Active

    Description:

    Activin-B Human Recombinant, Active

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-057

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

    More Info

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

    • Background

      An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active

      1. Abstract

      Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.

      2. Introduction

      The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.

      3. Structure and Synthesis of Activin-B

      Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.

      4. Biological Functions of Activin-B

      Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.

      5. Activin-B in Regenerative Medicine

      Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.

      6. Activin-B and Reproductive Health

      Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.

      7. Activin-B in Cancer

      Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.

      8. Conclusion and Future Perspectives

      Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin B Protein?
      The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

      What is the endotoxin level for Activin B Protein?
      The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B Protein be used in?
      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Activin B Human Active
  • View Data Sheet

    Name :

    TFPI Human, Sf9

    Description:

    Tissue Factor Pathway Inhibitor Human Recombinant, Sf9

    Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.

    Product # :

    PRO-2441

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    Description

    TFPI Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 285 amino acids (29-304a.a.) and having a molecular mass of 33kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TFPI is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TFPI protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TFPI is a protease inhibitor which controls the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process starts with the creation of a factor VIIa-TF complex, that proteolytically triggers additional proteases (factors IX and X) and eventually results in a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly located in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. A number of alternatively spliced transcript variants of this gene have are known, however the full-length nature of several of these variants were not yet established.

    • Synonyms

      Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      ADPDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNMH HHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tfpi Protein
  • View Data Sheet

    Name :

    ANGPTL3 Human

    Description:

    Angiopoietin Like Protein 3 Human Recombinant

    Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    Product # :

    CYT-248

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    The ANGPTL3 Human Recombinant is produced with N-terminal fusion of His-Tag. The Angiopoietin-like protein 3 His Tagged Fusion Protein is 26kDa containing 207 amino acid residues of the ANGPTL3 Human (26-233 a.a.) and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    ANGPTL3 Human filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Angiopoietin 5 purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.

    • Synonyms

      Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    • Stability

      Store lyophilized ANGPTL3 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Angiopoietin 5 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 0.1M Acetate buffer pH-4 and let the lyophilized pellet of ANGPTL3 Human dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of Angiopoietin 5 is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP.

    • Background

      Angiopoietin-Like Protein 3 Human Recombinant: An Emerging Target in Metabolic and Cardiovascular Disorders

      Abstract:


      Angiopoietin-like protein 3 (ANGPTL3) is a key regulator of lipid metabolism and has garnered considerable attention for its involvement in metabolic and cardiovascular disorders. ANGPTL3 plays a crucial role in lipid homeostasis, including the regulation of triglycerides, cholesterol, and lipoprotein metabolism. The availability of human recombinant ANGPTL3 protein has provided a valuable tool for investigating its biological functions and therapeutic potential. This review aims to provide a comprehensive overview of the role of ANGPTL3 in metabolic disorders, cardiovascular diseases, and lipid metabolism, highlighting the potential of ANGPTL3 human recombinant protein as a therapeutic target.

      Introduction:


      Metabolic disorders, such as dyslipidemia and obesity, significantly contribute to the development of cardiovascular diseases. ANGPTL3, a member of the angiopoietin-like protein family, has emerged as a key player in lipid metabolism and cardiovascular health. ANGPTL3 regulates lipoprotein metabolism, affecting triglyceride-rich lipoproteins, low-density lipoproteins (LDL), and high-density lipoproteins (HDL).

      Molecular Mechanisms of ANGPTL3 Action:


      ANGPTL3 exerts its effects through inhibition of lipoprotein lipase (LPL) and endothelial lipase (EL), key enzymes involved in lipoprotein metabolism. By inhibiting LPL and EL activities, ANGPTL3 increases plasma triglyceride and LDL cholesterol levels. ANGPTL3 also influences hepatic cholesterol metabolism and HDL metabolism through modulation of the receptor-mediated uptake of lipoproteins.

      Role of ANGPTL3 in Metabolic Regulation:


      ANGPTL3 plays a critical role in metabolic regulation, particularly in lipid metabolism and dyslipidemia. Loss-of-function mutations in the ANGPTL3 gene result in decreased plasma triglycerides, LDL cholesterol, and total cholesterol levels, highlighting the potential therapeutic relevance of ANGPTL3 inhibition. Conversely, elevated ANGPTL3 levels are associated with increased cardiovascular risk and atherogenic lipid profiles.

      ANGPTL3 in Cardiovascular Health and Disease:


      ANGPTL3 has emerged as a key modulator of cardiovascular diseases, including atherosclerosis and coronary artery disease. ANGPTL3 influences vascular endothelial function, inflammation, and plaque formation through its effects on lipoprotein metabolism and lipid accumulation. Inhibition of ANGPTL3 has shown promising results in preclinical studies, reducing atherosclerosis and improving cardiovascular outcomes.

      Therapeutic Potential of ANGPTL3 Human Recombinant Protein:


      The development of ANGPTL3 human recombinant protein provides a novel avenue for therapeutic interventions targeting metabolic and cardiovascular disorders. Inhibition of ANGPTL3 using monoclonal antibodies or other approaches has demonstrated efficacy in lowering plasma lipid levels, particularly triglycerides and LDL cholesterol. Clinical trials investigating the safety and efficacy of ANGPTL3 inhibition are underway.

      Conclusion:


      ANGPTL3 is a key regulator of lipid metabolism and a promising therapeutic target for metabolic and cardiovascular disorders. The availability of ANGPTL3 human recombinant protein has facilitated in-depth investigations into its biological functions and therapeutic potential. Targeting ANGPTL3 holds promise for improving lipid profiles, reducing cardiovascular risk, and managing metabolic disorders.

      What is the molecular weight/Mw of ANGPTL3 Protein?
      ANGPTL3 Protein has a total Mw of 26kDa.

      What is the source or expression system of ANGPTL3 Protein?
      Escherichia Coli.

      What is the Purity of ANGPTL3 Protein?
      ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL3 Protein?
      The biological functionality of ANGPTL3 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL3 Protein?
      MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP.

      What applications can ANGPTL3 Protein be used in?
      ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL3 Protein?
      The endotoxin level is minimal, ANGPTL3 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Angptl3 Human
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