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Search results

1000 results found for “interleukin 8 (cxcl8)”

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  • View Data Sheet

    Name :

    GM-CSF Human, Pichia

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    Product # :

    CYT-324

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.

    Purity

    Greater than 97.0% as determined by1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

    Citations

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O 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-Pro-Ala-Arg-Ser.

    • Background

      What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.

      What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

      What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

      What applications can GM-CSF HUMAN, PICHIA Protein be used in?
      GM-CSF HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
      The endotoxin level is minimal, GM-CSF HUMAN, PICHIA 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.

    Gm Csf Human Pichia
  • View Data Sheet

    Name :

    CMV Pp150

    Description:

    Cytomegalo Virus Pp150 (UL32) Recombinant

    Product # :

    CMV-216

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    Description

    The E.Coli derived recombinant protein contains the CMV Pp150 (UL32) immunodominant regions, 1011-1048 amino acids.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris pH 8.0, 1mM EDTA and 50% glycerol.

    Purity

    CMV Pp150 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV Pp150 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      CMV Pp65 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of CMV-infected individuals.

    • Purification Method

      CMV Pp150 was 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.

    Cmv Pp150
  • View Data Sheet

    Name :

    FSTL1 Human

    Description:

    Follistatin Like 1 Human Recombinant

    Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.

    Product # :

    CYT-792

    Price :

    Quantity :

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    Description

    FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FSTL1  Human SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.

    • Synonyms

      Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.

    • 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 MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.

    • Background

      What is the molecular weight/Mw of FSTL1 HUMAN Protein?
      FSTL1 HUMAN Protein has a total Mw of 34.9kDa.

      What is the source or expression system of FSTL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FSTL1 HUMAN Protein?
      FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FSTL1 HUMAN Protein?
      The biological functionality of FSTL1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of FSTL1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.

      What applications can FSTL1 HUMAN Protein be used in?
      FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FSTL1 HUMAN Protein?
      The endotoxin level is minimal, FSTL1 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.

    Fstl1 Human
  • View Data Sheet

    Name :

    CSK Antibody

    Description:

    C-Src Tyrosine Kinase, Mouse Anti Human

    Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.

    Product # :

    ANT-693

    Price :

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    Formulation

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

    Citations

    More Info

    • Introduction

      C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.

    • Synonyms

      Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CSK mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSK amino acids 1-450 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT7C6AT.

    • Applications

      CSK antibody has been tested by ELISA, Western blot analysis 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

      CSK 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.

    Csk Antibody
  • View Data Sheet

    Name :

    OSTF1 Antibody

    Description:

    Osteoclast Stimulating Factor-1, Mouse Anti Human

    SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    Product # :

    ANT-056

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    • More Info
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    Formulation

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

    Citations

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    • Introduction

      OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

    • Synonyms

      SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    • Immunogen

      Anti-human OSTF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human OSTF1 amino acids 1-217 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT9G4AT.

    • Applications

      OSTF1 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

      OSTF1 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.

    Ostf1 Antibody
  • View Data Sheet

    Name :

    Visfatin Antibody

    Description:

    Visfatin, Mouse Anti Human

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    ANT-368

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    Formulation

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

    Citations

    More Info

    • Introduction

      Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It h

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Immunogen

      Anti-human Visfatin mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Visfatin amino acids 1-491 purified from E. coli.

    • Ig Subclass

      Mouse IgG1heavy chain and κ light chain.

    • Clone

      P4D5AT.

    • Applications

      Visfatin 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.

    • 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

      Visfatin 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.

    Visfatin Antibody
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

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

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    Citations

    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, insulin resistance, 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 DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 TNF-a 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.

    Tnf Alpha Mouse
  • View Data Sheet

    Name :

    TNF a Human, Sf9

    Description:

    Tumor Necrosis Factor-alpha Human Recombinant, Sf9

    Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

    Product # :

    CYT-903

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    Description

    TNF a produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (77-233a.a.) and having a molecular mass of 18.1kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TNF a is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNF a protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined bySDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. 
    The ED50 for this effect is ≤ 0.2 ng/ml.

    Citations

    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, insulin resistance, and cancer.

    • Synonyms

      Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

    • 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

      VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIALHHH HHH.

    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.

    Tnf A Human Sf9
  • View Data Sheet

    Name :

    IRF5 Human

    Description:

    IFN Regulatory Factor-5 Human Recombinant

    IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    Product # :

    CYT-816

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    Description

    IRF5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (176-240a.a) and having a molecular mass of 10.7kDa.IRF5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IRF5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    SDS-PAGE

    IRF5 Human - Product image 1

    Citations

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    • Introduction

      IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.

    • Synonyms

      IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

    • Background

      What is the molecular weight/Mw of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein has a total Mw of 10.7kDa.

      What is the source or expression system of IRF5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IRF5 HUMAN Protein?
      The biological functionality of IRF5 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IRF5 HUMAN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

      What applications can IRF5 HUMAN Protein be used in?
      IRF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IRF5 HUMAN Protein?
      The endotoxin level is minimal, IRF5 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.

    Irf 5 Human
  • View Data Sheet

    Name :

    TRIM21 Human Biotin

    Description:

    Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated

    52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    Product # :

    PRO-2559

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    Description

    TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TRIM21 solution is supplied in 20mM HEPES pH-7.6, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

    • Synonyms

      52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Ro52 Human
  • View Data Sheet

    Name :

    IFNG Human, His

    Description:

    Interferon-Gamma Human Recombinant, His Tag

    Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-478

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    Description

    IFN-Gamma Human Recombinant produced in E.Coli is a single, glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) without cysteine residues and having a molecular mass of 18.5kDa (confirmed by MALDI-TOF). IFN-Gamma is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interferon-g is supplied in phosphate-buffered Saline (pH 7.4).

    Purity

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

    SDS-PAGE

    IFNG  Human - Product image 1

    Citations

    More Info

    • 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

      Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

    • Background

      What is the molecular weight/Mw of IFNG HUMAN, HIS Protein?
      IFNG HUMAN, HIS Protein has a total Mw of 18.5kDa.

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

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

      What is the Biological Activity of IFNG HUMAN, HIS Protein?
      The biological functionality of IFNG HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IFNG HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

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

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

    Interferon Gamma Human His
  • View Data Sheet

    Name :

    Myostatin Propeptide Human, HEK

    Description:

    Myostatin Propeptide Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-936

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    Description

    Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

    Source

    HEK 293.

    Formulation

    Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • 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

      NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

    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.

    Myostatin Propeptide Human Hek
  • View Data Sheet

    Name :

    Cor a 8.0101

    Description:

    Non-specific Lipid-Transfer Protein Cor a 8 Recombinant

    nsLTP Cor a 8, LTP Cor a 8.

    Product # :

    ALR-020

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    Description

    Recombinant Non-specific Lipid-Transfer Protein Cor a 8 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 11kDa.Cor a 8.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Cor a 8.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Nonspecific lipid transfer proteins (nsLTPs) are expressed throughout the plant tissues. They have a typical cysteine pattern forming disulfide bonds and are important allergens in fruits and tree nuts. Sensitization to nsLTP Cor a 8.0101 is more frequent among patients with hazelnut allergy in the Mediterranean area than the northern parts of Europe.

    • Synonyms

      nsLTP Cor a 8, LTP Cor a 8.

    • 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.Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples

    • Applications

      Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.

    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.

    Cor A 80101
  • View Data Sheet

    Name :

    CA8 Human

    Description:

    Carbonic Anhydrase 8 Human Recombinant

    Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.

    Product # :

    ENZ-235

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    Description

    CA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-290) and having a molecular mass of 35.5kDa.CA8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CA8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).

    • Synonyms

      Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.

    • 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 MGSHMADLSF IEDTVAFPEK EEDEEEEEEG VEWGYEEGVE WGLVFPDANG EYQSPINLNS REARYDPSLL DVRLSPNYVV CRDCEVTNDG HTIQVILKSK SVLSGGPLPQ GHEFELYEVR FHWGRENQRG SEHTVNFKAF PMELHLIHWN STLFGSIDEA VGKPHGIAII ALFVQIGKEH VGLKAVTEIL QDIQYKGKSK TIPCFNPNTL LPDPLLRDYW VYEGSLTIPP CSEGVTWILF RYPLTISQLQ IEEFRRLRTH VKGAELVEGC DGILGDNFRP TQPLSDRVIR AAFQ

    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.

    Ca8 Human
  • View Data Sheet

    Name :

    CTGF Human, HEK

    Description:

    Connective Tissue Growth Factor Human Recombinant , HEK

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

    Product # :

    CYT-687

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    Description

    The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.

    Source

    HEK293 cells.

    Formulation

    CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
      CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
      Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
      The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
      Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
      In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
      CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

    • 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

      QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

    • Background

      What is the molecular weight/Mw of CTGF Protein?
      CTGF Protein has a total Mw of 36kDa.

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

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

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

      What is the amino acid sequence of CTGF Protein?
      QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

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

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

    Ctgf Humam Hek
  • View Data Sheet

    Name :

    SHH Human

    Description:

    Sonic HedgeHog Human Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-676

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    Description

    Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.

    Source

    Escherichia Coli.

    Formulation

    SHH is lyophilized from 10mM Na3PO4, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.

    Citations

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized SHH in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP

    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.

    Sonic Hedgehog Human
  • View Data Sheet

    Name :

    MIF Human, Active

    Description:

    Macrophage Migration Inhibitory Factor Human Recombinant (Active)

    Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    Product # :

    CYT-596

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    Description

    MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.

    Purity

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

    Biological Activity

    Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.

    Citations

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIF-protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF-protein 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 MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.

    • Amino Acid Sequence

      MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
      AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
      INYYDMNAANVGWNNSTFA.

    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.

    Mif Human Active
  • View Data Sheet

    Name :

    DHH (C23II) Human

    Description:

    Desert Hedgehog (C23II) Human Recombinant

    HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    Product # :

    CYT-362

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    Description

    DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 15-45 μg/ml.

    Citations

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

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    Dhh C23Ii Human
  • View Data Sheet

    Name :

    4 1BBL Human

    Description:

    4-1BB Ligand Human Recombinant

    CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    Product # :

    CYT-149

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    Description

    4 1BBL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 19.5kDa.The 4 1BBL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Determined by the dose-dependent stimulation of IL-8 production by human PBMC. The ED50 for this effect is 5-10ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

    Citations

    More Info

    • Introduction

      4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin.

    • Synonyms

      CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized 4 1BBL although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 4 1BBL should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized 4 1BBL in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      REGPELSPDD PAGLLDLRQG MFAQLVAQNV LLIDGPLSWY SDPGLAGVSL TGGLSYKEDT KELVVAKAGV YYVFFQLELR RVVAGEGSGS VSLALHLQPL RSAAGAAALA LTVDLPPASS EARNSAFGFQ GRLLHLSAGQ RLGVHLHTEA RARHAWQLTQ GATVLGLFRV TPEIPAGLPS PRSE

    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 1Bbl Human
  • View Data Sheet

    Name :

    Betacellulin Human

    Description:

    Betacellulin Human Recombinant

    Product # :

    CYT-330

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    Description

    Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Human Recombinant 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.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

    • Background

      Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine

      Introduction

      In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.

      BTC: The Architect of Cellular Revitalization

      BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.

      Crafting the Alchemist: Pioneering Methodologies

      Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.

      Unveiling the Biological Tapestry

      Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.

      A Flourish of Results

      The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.

      Charting a Transformative Future

      As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.

      What is the molecular weight/Mw of BTC Protein?
      BTC Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BTC Protein?
      The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

      What is the amino acid sequence of BTC Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

    Betacellulin Human
  • View Data Sheet

    Name :

    LIF Human

    Description:

    Leukemia Inhibitory Factor Human Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-644

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    Description

    Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.

    • Background

      Leukemia Inhibitory Factor (LIF) Background

      Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.

      LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.

      Function and Applications of LIF

      LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.

      Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.

      Structure and Interactions

      LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

    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.

    Lif Human
  • View Data Sheet

    Name :

    AIF1L Human

    Description:

    Allograft Inflammatory Factor 1 Like Human Recombinant

    Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.

    Product # :

    CYT-007

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • source
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    • More Info
    • sds-page
    • Citations

    Description

    AIF1L produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150a.a.) and having a molecular mass of 19.2kDa.AIF1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AIF1L protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    sds-page

    AIF1L sds-page - Product image 1

    Citations

    More Info

    • Synonyms

      Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.

    • 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 MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.

    • Background

      Allograft Inflammatory Factor 1-Like Human Recombinant: Investigating its Role in Immune Responses and Potential Therapeutic Applications

      1. Abstract

      This paper seeks to provide an in-depth overview of Allograft Inflammatory Factor 1-Like Human Recombinant (AIF-1L), a significant protein involved in the regulation of inflammatory responses. By delving into the structure, biological functions, and pathological implications of AIF-1L, we attempt to shed light on its potential as a therapeutic target in immune-mediated disorders.

      2. Introduction

      AIF-1L belongs to the allograft inflammatory factor protein family and is implicated in immune responses. With its intricate interaction with a multitude of immune cells and involvement in various inflammatory and immune-related diseases, it serves as a pivotal point of interest for therapeutic intervention research.

      3. Structure and Signaling of AIF-1L

      AIF-1L shares a conserved EF-hand calcium-binding motif with its counterpart AIF-1, suggesting similar calcium-dependent activities. While its signaling pathway remains largely elusive, the protein is believed to modulate macrophage activation, an integral part of immune response regulation.

      4. Biological Functions of AIF-1L

      AIF-1L is fundamentally involved in immune response modulation, especially in the context of macrophage activation. It plays key roles in managing inflammation, cell proliferation, survival, and differentiation.

      5. AIF-1L in Disease Pathology

      AIF-1L is linked with a range of inflammatory and immune-related disorders, including but not limited to rheumatoid arthritis, atherosclerosis, and certain cancers. This association underscores its profound physiological relevance and potential as a therapeutic target.

      6. Therapeutic Potential of AIF-1L

      Given its central role in immune responses, AIF-1L presents a promising target for therapeutic strategies. Manipulating AIF-1L activity could pave the way for novel treatments of various inflammatory and immune-mediated diseases.

      7. Conclusion and Future Perspectives

      Though our comprehension of AIF-1L has made significant strides, there is still much terrain left to explore. Future research directed at the precise molecular mechanisms and pathological roles of AIF-1L will undoubtedly contribute to the development of novel therapeutic strategies.

      What is the molecular weight/Mw of AIF1L Protein?
      AIF1L Protein has a total Mw of 19.2kDa.

      What is the source or expression system of AIF1L Protein?
      Escherichia Coli.

      What is the Purity of AIF1L Protein?
      AIF1L Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of AIF1L Protein?
      The biological functionality of AIF1L Protein will be determined in the future.

      What is the amino acid sequence of AIF1L Protein?
      MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.

      What applications can AIF1L Protein be used in?
      AIF1L Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for AIF1L Protein?
      The endotoxin level is minimal, AIF1L 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.

    Aif1L Human
  • View Data Sheet

    Name :

    MIP 1a Antibody

    Description:

    Macrophage Inflammatory-1 alpha, Mouse Anti-Human

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    Product # :

    ANT-118

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • formulation
    • More Info
    • Citations

    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1(IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    • Solubility

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

    • Immunogen

      r.Human MIP1-a.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      YNR-HMIP1a.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation.

    • Titer

      By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange.

    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.

    Mip 1A Antibody
  • View Data Sheet

    Name :

    IFN b Antibody

    Description:

    Interferon-beta, Mouse Anti-Human

    Leukocyte interferon, B cell interferon, Type I interferon, IFNB1, IFB, IFF, IFNB, IFN-b 1a MGC96956.

    Product # :

    ANT-185

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • formulation
    • More Info
    • Citations

    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

    More Info

    • Introduction

      Interferon-beta has antiviral, antibacterial and anticancer activities.

    • Synonyms

      Leukocyte interferon, B cell interferon, Type I interferon, IFNB1, IFB, IFF, IFNB, IFN-b 1a MGC96956.

    • Solubility

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

    • Immunogen

      r.Human IFN-b.

    • Ig Subclass

      Mouse IgG.

    • Clone

      NYRhIFN-b.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • 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.

    Interferon Beta Antibody
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