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1000 results found for “anti human cytokine”

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  • View Data Sheet

    Description:

    4-1BB Receptor Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    Product # :

    CYT-916

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    Description

    4-1BBR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 172 amino acids (24-187 a.a.) and having a molecular mass of 18.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions). 4-1BBR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    4-1BBR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    • 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

      VQNSCDNCQP GTFCRKYNPV CKSCPPSTFS SIGGQPNCNI CRVCAGYFRF KKFCSSTHNA ECECIEGFHC LGPQCTRCEK DCRPGQELTK QGCKTCSLGT FNDQNGTGVC RPWTNCSLDG RSVLKTGTTE KDVVCGPPVV SFSPSTTISV TPEGGPGGHS LQVLLEHHHH HH.

    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.

    4-1BBR Mouse
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    Description:

    Immunoglobulin-M Human

    Product # :

    PRO-2745

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    Description

    Human Immunoglobulin-M produced in human plasma having a molecular mass of 950kDa.

    Source

    Human plasma.

    Formulation

    IgM solution (1.98mg/ml) contains 50mM TRIS buffer, pH 8.0, 0.2M NaCl and 0.05% NaN3.

    Purity

    Greater than 95.0%.

    More Info

    • Introduction

      Immunoglobulin M (IgM) is a basic antibody produced by B cells. IgM is the first antibody to emerge in response to initial exposure to an antigen. IgM antibodies are found in the blood and lymph fluid and are the third most widespread serum Ig. Immunoglobulin M (IgM), being the 3rd most widespread serum Ig and exists in two forms- mostly as a pentamer (970kDa) but also as a hexamer. The pentameric IgM has 10 binding sites since each monomer has two antigen binding sites. Due to distance constraints in the hexameric complex, the J chain is found in pentameric IgM but not in the hexameric form. IgM antibodies, which appear early in the course of an infection, typically reappear to a smaller extent after additional exposure. IgM, as opposed to IgG antibodies, do not pass across the human placenta. These properties of IgM make it suitable for the diagnosis of infectious diseases.

    • Physical Appearance

      Sterile Filtered 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.

    • Human Virus Test

      Human Immunoglobulin-M has been tested and certified negative for antibodies to HIV-1, HIV-2, anti-HBc, 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.

    Igm Human
  • View Data Sheet

    Description:

    Epiregulin Human Recombinant, HEK

    EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    Product # :

    CYT-1206

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    Description

    EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

    More Info

    • Introduction

      "Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."

    • Synonyms

      EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    • 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

      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 32.6kDa.

      What is the source or expression system of EREG Protein?
      HEK293 cells.

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

      What is the Biological Activity of EREG Protein?
      Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

      What is the amino acid sequence of EREG Protein?
      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

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

      What is the endotoxin level for EREG Protein?
      The endotoxin level is minimal, EREG 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.

    Ereg Human
  • View Data Sheet

    Description:

    Trefoil Factor-1 Human Recombinant, His Tag

    TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    Product # :

    CYT-610

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    Description

    TFF-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids (25-84) which includes a 10 amino acid His Tag and having a total molecular mass of 7.9 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF1 His Tag protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

    • Synonyms

      TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 His Tag 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 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 in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF.

    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.

    Tff1 Human His
  • View Data Sheet

    Description:

    Neutrophil Cytosolic Factor 4 Human Recombinant

    Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.

    Product # :

    PRO-1258

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    Description

    NCF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-339 a.a) and having a molecular mass of 41.1kDa.NCF4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neutrophil Cytosolic Factor 4 (NCF4) is a cytosolic regulatory factor of the superoxide-producing phagocyte NADPH-oxidase, which is a multicomponent enzyme system imperative for host defense. The NCF4 protein is preferentially expressed in cells of myeloid lineage. NCF4 interacts mainly with neutrophil cytosolic factor 2 (NCF2/p67-phox) to create a complex with neutrophil cytosolic factor (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex subsequently activates flavocytochrome b, the membrane-integratedcatalytic core of the enzyme system. The PX domain of the NCF4 protein can bind phospholipid products of the PI(3) kinase, suggesting its part in PI(3) kinase-mediated signaling events. The phosphorylation of the NCF4 protein negatively regulates the enzyme activity.

    • Synonyms

      Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.

    • 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 MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE IAEMRIPALN AYMKSLLSLP VWVLMDEDVR IFFYQSPYDS EQVPQALRRL RPRTRKVKSV SPQGNSVDRM AAPRAEALFD FTGNSKLELN FKAGDVIFLL SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL RCYYYEDTIS TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP.

    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.

    Ncf4 Human
  • View Data Sheet

    Description:

    Janus Kinase 2, Mouse Anti Human

    Tyrosine-protein kinase JAK2, Janus kinase 2, JAK-2, JAK2, Janus kinase 2 (a protein tyrosine kinase), JTK10.

    Product # :

    ANT-644

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Janus Kinase 2 (JAK2) is a protein tyrosine kinase which takes part in a specific subset of cytokine receptor signaling pathways such as cell growth, development, differentiation or histone modifications. JAK2 is linked with the prolactin receptor and is necessary for responses to gamma interferon. Mice which do not express an active protein for JAK2 show embryonic lethality associated with the absence of definitive erythropoiesis.

    • Synonyms

      Tyrosine-protein kinase JAK2, Janus kinase 2, JAK-2, JAK2, Janus kinase 2 (a protein tyrosine kinase), JTK10.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human JAK2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human JAK2 amino acids 1014-1132 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT53B7AT.

    • Applications

      JAK2 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      JAK2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Jak2 Antibody
  • View Data Sheet

    Description:

    Angiopoietin-like Protein 4 Human Recombinant, HEK

    ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.

    Product # :

    CYT-698

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    Description

    The ANGPTL4 Human Recombinant is manufactured with C-terminal fusion of 11 amino acid FLAG Tag. The ANGPTL4 Flag -Tagged Fusion Protein is a 44.2kDa protein containing 392 amino acid residues of the Angiopoietin-like Protein 4 and 11 additional amino acid residues - Flag Tag (underlined).

    Source

    HEK293.

    Formulation

    Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The fasting-induced adipose factor (FIAF, ANGPTL4, PGAR, HFARP) was identified as an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. At the protein level, in human and mouse blood plasma, FIAF was found to be present both as a native protein and in a truncated form. Differentiation of mouse 3T3-L1 adipocytes was associated with the production of truncated FIAF, whereas in human white adipose tissue and SGBS adipocytes, only the native FIAF could be detected. Interestingly, the truncated FIAF was produced by human liver.
      Experimental data suggest that FIAF is mainly presented in human blood plasma in a truncated form (FIAF-S2), whose level is increased by fenofibrate treatment. Levels of both truncated and native FIAF showed marked inter individual variation but were not associated with body mass index and were not influenced by prolonged semistarvation.

    • Synonyms

      ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Angiopoietin-like Protein 4 Human recombinant 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

      Add pyrogen free water to a working concentration of 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 in the cell culture.

    • Amino Acid Sequence

      GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.

    • Applications

      Western blotting.

    • Background

      What is the molecular weight/Mw of ANGPTL4 Protein?
      ANGPTL4 Protein has a total Mw of 44.2kDa.

      What is the source or expression system of ANGPTL4 Protein?
      HEK293.

      What is the Purity of ANGPTL4 Protein?
      ANGPTL4 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL4 Protein?
      The biological functionality of ANGPTL4 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL4 Protein?
      GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.

      What applications can ANGPTL4 Protein be used in?
      ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL4 Protein?
      The endotoxin level is minimal, ANGPTL4 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.

    Angptl4 Human Hek
  • View Data Sheet

    Description:

    Resistin Rat Recombinant, His Tag

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-458

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    Description

    Resistin Rat Recombinant is manufactured with N-terminal fusion of His tag. Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid residues of the Resistin Rat and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Mouse resistin is expressed as a 114 amino acid prepeptide; its hydrofobic Nterminal 20 amino acid signal peptide is cleaved before its secretion. Mouse resistin circulates in blood as a homodimeric protein consisting of two 94 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMPSMS LCPMDEAISK KINQDFSSLL PAAMKNTVLH CWSVSSRGRL ASCPEGTTVT SCSCGSGCGS WDVREDTMCH CQCGSIDWTA ARCCTLRVGS.

    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.

    Resistin Rat
  • View Data Sheet

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-220

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.GCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 GCSF in sterile 20mM AcOH 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 of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein has a total Mw of 18.8kDa.

      What is the source or expression system of GDF15 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN, HIS Protein?
      The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

      What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is composed from 175 amino acids.

      What applications can GDF15 HUMAN, HIS Protein be used in?
      GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.

    • Protein content

      GCSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GCSF as a Reference Standard.

    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.

    G Csf Human
  • View Data Sheet

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

    Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    Product # :

    CYT-938

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    Description

    BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

    Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

    More Info

    • Introduction

      Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.

    • Synonyms

      Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

    • Background

      Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-13 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.

      Potential Therapeutic Applications:

      BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of GDF6 Protein?
      GDF6 Protein has a total Mw of 27.1kDa.

      What is the source or expression system of GDF6 Protein?
      Escherichia Coli.

      What is the Purity of GDF6 Protein?
      GDF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF6 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

      What is the amino acid sequence of GDF6 Protein?
      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

      What applications can GDF6 Protein be used in?
      GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF6 Protein?
      The endotoxin level is minimal, GDF6 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.

    Bmp13 Human
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Rat Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-393

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    Description

    Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 IU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

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    Tnf Alpha Rat
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein-2 Human Recombinant, Monomer

    BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    Product # :

    CYT-627

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    Description

    Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. The BMP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-2 solution contains 10mM NaAc pH=3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

    • Synonyms

      BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP2 Protein?
      Escherichia Coli.

      What is the Purity of BMP2 Protein?
      BMP2 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP2 Protein?
      The biological functionality of BMP2 Protein will be determined in the future.

      What is the amino acid sequence of BMP2 Protein?
      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

      What applications can BMP2 Protein be used in?
      BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP2 Protein?
      The endotoxin level is minimal, BMP2 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.

    Bmp 2 Human Monomer
  • View Data Sheet

    Description:

    WNT1 Inducible Signaling Pathway Protein 2 Human Recombinant

    WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    Product # :

    CYT-970

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    Description

    WISP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 24.4kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WNT1-inducible-signaling pathway protein 2 (WISP2) belongs to the WNT1 inducible signaling pathway (WISP) protein subfamily, which belongs to the connective tissue growth factor (CTGF) family. The CTGF family members are characterized by 4 conserved cysteine-rich domains: insulin-like growth factor-binding domain, von Willebrand factor type C module, thrombospondin domain and C-terminal cystine knot-like (CT) domain. WISP2 protein lacks the CT domain which is implicated in dimerization binding. WISP2 is possibly involved in bone remodeling. WISP2 is expressed in primary osteoblasts and fibroblasts. WISP2 stimulates osteoblast adhesion and inhibits osteocalcin production. WISP2 expression in colon tumors is reduced while the other 2 WISP members are overexpressed in colon tumors. WISP2 may play an imperative role in modulating bone turnover.

    • Synonyms

      WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized WISP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution WISP-2 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 WISP-2 in sterile 10mM acetic acidnot less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQLCPTPCTC PWPPPRCPLG VPLVLDGCGC CRVCARRLGE PCDQLHVCDA SQGLVCQPGA GPGGRGALCL LAEDDSSCEV NGRLYREGET FQPHCSIRCR CEDGGFTCVP LCSEDVRLPS WDCPHPRRVE VLGKCCPEWV CGQGGGLGTQ PLPAQGPQFS GLVSSLPPGV PCPEWSTAWG PCSTTCGLGM ATRVSNQNRF CRLETQRRLC LSRPCPPSRG RSPQNSAF.

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    Wisp2 Human
  • View Data Sheet

    Description:

    Apolipoprotein A-I Human Recombinant

    Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

    Product # :

    CYT-750

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    Description

    Apolipoprotein A-I Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids and having a molecular mass of 28.1kDa.The APOA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The APOA1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.

    • Synonyms

      Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Apolipoprotein A-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOA1 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 APOA1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.

    • Background

      Apolipoprotein A-I Human Recombinant: A Promising Therapeutic Agent for Cardiovascular Diseases

      Abstract:


      Cardiovascular diseases (CVDs) remain a leading cause of mortality worldwide. Dyslipidemia, characterized by abnormal lipid profiles, is a significant risk factor for the development of CVDs. Apolipoprotein A-I (ApoA-I) is the primary protein component of high-density lipoprotein (HDL), known as the "good cholesterol." ApoA-I plays a crucial role in reverse cholesterol transport, promoting the efflux of cholesterol from peripheral tissues to the liver for elimination. Recombinant ApoA-I offers a potential therapeutic strategy for enhancing HDL functionality and reducing CVD risk. This research paper aims to provide an overview of ApoA-I human recombinant, its production methods, and its therapeutic applications in cardiovascular medicine.

      Introduction


      Cardiovascular diseases and dyslipidemia
      Role of apolipoprotein A-I in reverse cholesterol transport
      Potential of ApoA-I human recombinant as a therapeutic agent

      Structure and Function of Apolipoprotein A-I


      Primary structure and domains of ApoA-I
      Functional properties of ApoA-I in reverse cholesterol transport
      Interaction with other lipoproteins and cellular receptors

      Production of Apolipoprotein A-I Human Recombinant


      Expression systems for recombinant ApoA-I
      Biotechnological methods for large-scale production
      Purification and characterization of recombinant ApoA-I

      Therapeutic Applications of Apolipoprotein A-I Human Recombinant


      Promotion of reverse cholesterol transport
      Anti-inflammatory and antioxidant effects
      Enhancement of endothelial function
      Cardioprotective effects in animal models

      Clinical Trials and Future Perspectives


      Phase I and II clinical trials
      Challenges and limitations
      Future directions and potential therapeutic combinations

      Conclusion


      Summary of the potential of ApoA-I human recombinant as a therapeutic agent for CVDs
      Importance of ongoing research and clinical trials

      What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
      APOLIPOPROTEIN A1 Protein has a total Mw of 28.1kDa.

      What is the source or expression system of APOLIPOPROTEIN A1 Protein?
      Escherichia Coli.

      What is the Purity of APOLIPOPROTEIN A1 Protein?
      APOLIPOPROTEIN A1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
      The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.

      What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
      DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.

      What applications can APOLIPOPROTEIN A1 Protein be used in?
      APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
      The endotoxin level is minimal, APOLIPOPROTEIN A1 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.

    Apoa1
  • View Data Sheet

    Description:

    Inhibitor of DNA Binding 2 Human Recombinant

    DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.

    Product # :

    PRO-1383

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    Description

    ID2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17kDa. ID2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ID2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Inhibitor of DNA Binding 2 (ID2) is a part of the inhibitor of DNA binding family, whose members are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative way by suppressing their heterodimerization partners through the HLH domains. ID2 play a role in negatively regulating cell differentiation and may be an inhibitor of tissue-specific gene expression.

    • Synonyms

      DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.

    • 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 MKAFSPVRSV RKNSLSDHSL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVS KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQNQASR TPLTTLNTDI SILSLQASEF PSELMSNDSK ALCG.

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    Id2 Human
  • View Data Sheet

    Description:

    Cell Death-Inducing DFFA-Like Effector C Human Recombinant

    Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    Product # :

    PRO-2026

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    Description

    CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.

    Source

    Escherichia Coli.

    Formulation

    CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.

    • Synonyms

      Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    • Physical Appearance

      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

      MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.

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    Cidec Human
  • View Data Sheet

    Description:

    VEGF Co-regulated Chemokine 1 Human Recombinant

    VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.

    Product # :

    CHM-019

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    Description

    CXCL17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4, containing 3% Trehalose.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.

    More Info

    • Introduction

      Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

    • Synonyms

      VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.

    • Background

      What is the molecular weight/Mw of CXCL17 HUMAN Protein?
      CXCL17 HUMAN Protein has a total Mw of 11.5kDa.

      What is the source or expression system of CXCL17 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL17 HUMAN Protein?
      CXCL17 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 HUMAN Protein?
      The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.

      What is the amino acid sequence of CXCL17 HUMAN Protein?
      SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.

      What applications can CXCL17 HUMAN Protein be used in?
      CXCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL17 HUMAN Protein?
      The endotoxin level is minimal, CXCL17 HUMAN 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.

    Cxcl17 Human
  • View Data Sheet

    Description:

    Cathelicidin Antimicrobial Peptide Human Recombinant

    CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    Product # :

    PRO-1405

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    Description

    CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.

    • Synonyms

      CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    • 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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

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    Camp Human
  • View Data Sheet

    Description:

    Cathepsin D, Mouse Anti Human

    Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    Product # :

    ANT-324

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    Formulation

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

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    • Introduction

      Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

    • Synonyms

      Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human CTSD mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CTSD amino acids 21-412 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P4G2AT.

    • Applications

      CTSD 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

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

    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.

    Ctsd Antibody
  • View Data Sheet

    Description:

    NF-kappa-B Inhibitor Alpha Human Recombinant

    Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.

    Product # :

    PRO-960

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    Description

    NFKBIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-317) and having a molecular mass of 37.7 kDa.NFKBIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NFKBIA belongs to the I-kappa-B family of proteins which is separated into four groups (IkB-a, IkB-b, IkB-g, IkB-e). NFKBIA inhibits the NFkB complex by binding and impounding it in the cytoplasm. When stimulated, NFKBIA is phosphorylated on serine residues targeting it for degradation by the ubiquitin pathway.

    • Synonyms

      Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.

    • 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 MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE DELPYDDCVF GGQRLTL

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    Nfkbia Human
  • View Data Sheet

    Description:

    Interferon-Gamma Equine Recombinant

    Interferon gamma, IFN-gamma, IFNG.

    Product # :

    CYT-739

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    Description

    Recombinant Equine Interferon-gamma produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 143 amino acids and having a molecular mass of 16.7kDa.The IFN-gamma Equine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

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    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

    • Synonyms

      Interferon gamma, IFN-gamma, IFNG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interferon-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 Interferon-gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ.

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    Interferon Gamma Equine
  • View Data Sheet

    Description:

    Bone Morphogenetic protein-5 Human Recombinant

    Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    Product # :

    CYT-660

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    • sds-page

    Description

    BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

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    • Introduction

      BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
      BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

    • Synonyms

      Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    • 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

      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

    • Background

      Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-5 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.

      Potential Therapeutic Applications:

      BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.

      What is the molecular weight/Mw of BMP5 Protein?
      BMP5 Protein has a total Mw of 15.7kDa.

      What is the source or expression system of BMP5 Protein?
      Escherichia Coli.

      What is the Purity of BMP5 Protein?
      BMP5 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP5 Protein?
      The biological functionality of BMP5 Protein will be determined in the future.

      What is the amino acid sequence of BMP5 Protein?
      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

      What applications can BMP5 Protein be used in?
      BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP5 Protein?
      The endotoxin level is minimal, BMP5 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.

    Bmp 5 Human
  • View Data Sheet

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Human Recombinant

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    PRO-1886

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    Description

    NCR3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (19-138 a.a) and having a molecular mass of 15.3kDa.NCR3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCR3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLWVSQPPEI RTLEGSSAFL PCSFNASQGR LAIGSVTWFR DEVVPGKEVR NGTPEFRGRL APLASSRFLH DHQAELHIRD VRGHDASIYV CRVEVLGLGV GTGNGTRLVV EKEHPQLGAG T

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    Ncr3 Human
  • View Data Sheet

    Description:

    CD21, Mouse Anti-Human, Biotin

    Complement receptor type 2, Cr2, Complement C3d receptor, Epstein-Barr virus receptor, EBV receptor, CD21 antigen, CR2, C3DR, CD21, SLEB9.

    Product # :

    ANT-258

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      CD21 is expressed strongly on mature B cells, follicular dentritic cells and weakly on immature thymocytes and T lymphocytes. In B-cell ontogeny, CD21 appears after the pre-B-stage, is maintained during peripheral B-cell development and is lost upon terminal differentiation into plasma cells. CD21 expression is also gradually lost after stimulation of B cells in vitro. CD21 functions as receptor for C3d, C3dg and iC3b Complement components, for EBV and for IFNalpha. CD21 binds to CD23 and associates with CD19, CD81 and Leu13 to form a large signal-transduction complex involved in B cell activation.

    • Synonyms

      Complement receptor type 2, Cr2, Complement C3d receptor, Epstein-Barr virus receptor, EBV receptor, CD21 antigen, CR2, C3DR, CD21, SLEB9.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified human B-Cells.

    • Ig Subclass

      Mouse IgG2a.

    • Clone

      hCD21.

    • Applications

      Staining antibody. For staining, use 10µl/1,000,000 cells.

    • Available Conjugates

      This antibody is also available unconjugated and FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/106 cells.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Protein-A.

    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.

    Cd21 Antibody Biotin