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Search results

934 results found for “Biglycan”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Insulin Human, His

    Description:

    Insulin Human Recombinant, His Tag

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.    

    Product # :

    CYT-1076

    Price :

    Quantity :

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    • source
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    Description

    Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.

    Citations

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • 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 MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN

    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.

    Insulin 2
  • View Data Sheet

    Name :

    GPC3 Human

    Description:

    Glypican-3 Human Recombinant

    Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.

    Product # :

    PRO-2423

    Price :

    Quantity :

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    Description

    GPC3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 544 amino acids (25-559a.a.) and having a molecular mass of 61.8kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GPC3 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GPC3 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.

    Citations

    More Info

    • Introduction

      Glypican-3 (GPC3) belongs to the glypican family, and is highly expressed in the lung, liver, and the kidney. In some tissues, GPC3 functionss as a tumor suppressor gene and an oncofetal protein. The Glypican-3 protein is currently considered as a tumor marker and potential target for immunotherapy. Glypican-3 binds to and inhibits the dipeptidyl peptidase activity of CD26, and it can also induce apoptosis in certain cell types. Deletion mutations in the GPC3 gene are linked with Simpson-Golabi-Behmel syndrome, aka Simpson dysmorphia syndrome.

    • Synonyms

      Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.

    • 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

      ADPQPPPPPP DATCHQVRSF FQRLQPGLKW VPETPVPGSD LQVCLPKGPT CCSRKMEEKY QLTARLNMEQ LLQSASMELK FLIIQNAAVF QEAFEIVVRH AKNYTNAMFK NNYPSLTPQA FEFVGEFFTD VSLYILGSDI NVDDMVNELF DSLFPVIYTQ LMNPGLPDSA LDINECLRGA RRDLKVFGNF PKLIMTQVSK SLQVTRIFLQ ALNLGIEVIN TTDHLKFSKD CGRMLTRMWY CSYCQGLMMV KPCGGYCNVV MQGCMAGVVE IDKYWREYIL SLEELVNGMY RIYDMENVLL GLFSTIHDSI QYVQKNAGKL TTTIGKLCAH SQQRQYRSAY YPEDLFIDKK VLKVAHVEHE ETLSSRRREL IQKLKSFISF YSALPGYICS HSPVAENDTL CWNGQELVER YSQKAARNGM KNQFNLHELK MKGPEPVVSQ IIDKLKHINQ LLRTMSMPKG RVLDKNLDEE GFESGDCGDD EDECIGGSGD GMIKVKNQLR FLAELAYDLD VDDAPGNSQQ ATPKDNEIST FHNLGNVHHH HHHH.

    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.

    Gpc3 Human
  • View Data Sheet

    Name :

    CMV Pp28

    Description:

    Cytomegalo Virus Pp28 (UL99) Recombinant

    Product # :

    CMV-212

    Price :

    Quantity :

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    • description
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    • formulation
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    • Citations

    Description

    The E.Coli derived recombinant protein contains the CMV Pp28 (UL99) immunodominant regions, 130-160 amino acids.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-Hcl pH 7.2, 1mM EDTA and 50% glycerol.

    Purity

    CMV Pp28 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.

    • Stability

      CMV Pp28 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      CMV Pp28 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

      Purified by GS-4B Sepharose-Affinity Purification.

    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 Pp28
  • View Data Sheet

    Name :

    NT 3 Human

    Description:

    Neurotrophin-3 Human Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    Product # :

    CYT-257

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.1% TFA.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

    Citations

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 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 standard solution of NT-3 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.

    Neurotrophin 3 Human
  • View Data Sheet

    Name :

    HSPA9 Human

    Description:

    Heat Shock 70kDa Protein 9 Human Recombinant

    Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.

    Product # :

    HSP-023

    Price :

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    • description
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    Description

    Recombinant Human HSPA9 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 654 amino acids (47-679) and having a molecular mass of 71 kDa.HSP9A is expressed with a 20 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSPA9 protein solution contains 20mM Tris-HCl, pH-8, 10% glycerol and 0.5mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HSPA9 is part of the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members that are also called heat-shock cognate proteins. HSPA9 encodes a heat-shock cognate protein that is involved in the control of cell proliferation and acts as a chaperone. HSPA9 was restricted to chromosome 5, band q31, a region that is often deleted in myeloid leukemias and myelodysplasia (MDS), making it a candidate tumor suppressor gene, which is consistent with the biological function of its murine homologue. HSPA9 supresses nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53.

    • Synonyms

      Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.

    • 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 MASEAIKGAV VGIDLGTTNS CVAVMEGKQA KVLENAEGAR TTPSVVAFTA DGERLVGMPA KRQAVTNPNN TFYATKRLIG RRYDDPEVQK DIKNVPFKIV RASNGDAWVE AHGKLYSPSQ IGAFVLMKMK ETAENYLGHT AKNAVITVPA YFNDSQRQAT KDAGQISGLN VLRVINEPTA AALAYGLDKS EDKVIAVYDL GGGTFDISIL EIQKGVFEVK STNGDTFLGG EDFDQALLRH IVKEFKRETG VDLTKDNMAL QRVREAAEKA KCELSSSVQT DINLPYLTMD SSGPKHLNMK LTRAQFEGIV TDLIRRTIAP CQKAMQDAEV SKSDIGEVIL VGGMTRMPKV QQTVQDLFGR APSKAVNPDE AVAIGAAIQG GVLAGDVTDV LLLDVTPLSL GIETLGGVFT KLINRNTTIP TKKSQVFSTA ADGQTQVEIK VCQGEREMAG DNKLLGQFTL IGIPPAPRGV PQIEVTFDID ANGIVHVSAK DKGTGREQQI VIQSSGGLSK DDIENMVKNA EKYAEEDRRK KERVEAVNMA EGIIHDTETK MEEFKDQLPA DECNKLKEEI SKMRELLARK DSETGENIRQ AASSLQQASL KLFEMAYKKM ASEREGSGSS GTGEQKEDQK EEKQ.

    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.

    Hspa9 Human
  • View Data Sheet

    Name :

    PRLR Human, Antagonist

    Description:

    Prolactin Receptor Antagonist Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-1254

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    Description

    Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).

    Citations

    More Info

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr

    • Background

      Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    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.

    Prolactin Receptor Antagonist
  • View Data Sheet

    Name :

    CTSD Human

    Description:

    Cathepsin-D Human Recombinant

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

    Product # :

    ENZ-378

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    Description

    CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE

    Citations

    More Info

    • 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 clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH

    • Enzymatic Activity

      > 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

    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 Human
  • View Data Sheet

    Name :

    WHSC2 Human

    Description:

    Wolf-Hirschhorn Syndrome Candidate 2 Human Recombinant

    Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.

    Product # :

    PRO-062

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    Description

    WHSC2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 559 amino acids (1-539 a.a.) and having a molecular mass of 60.6kDa. The WHSC2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WHSC2 solution (0.25 mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      WHSC2 (NELF-A) is a protein factor required for DRB-sensitive transcription. WHSC2 is one of the 5 components of the multisubunit NELF complex which cooperates with DSIF to repress RNA polymerase II elongation. The Wolf-Hirschhorn syndrome is a multiple malformation syndrome characterized by mental and developmental defects resulting from a hemizygous deletion of the distal short arm of chromosome 4 (4p16.3).

    • Synonyms

      Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.

    • 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 MPGQRRALSP KMASMRESDT GLWLHNKLGA TDELWAPPSI ASLLTAAVID NIRLCFHGLS SAVKLKLLLG TLHLPRRTVD EMKGALMEII QLASLDSDPW VLMVADILKS FPDTGSLNLE LEEQNPNVQD ILGELREKVG ECEASAMLPL ECQYLNKNAL TTLAGPLTPP VKHFQLKRKP KSATLRAELL QKSTETAQQL KRSAGVPFHA KGRGLLRKMD TTTPLKGIPK QAPFRSPTAP SVFSPTGNRT PIPPSRTLLR KERGVKLLDI SELDMVGAGR EAKRRRKTLD AEVVEKPAKE ETVVENATPD YAAGLVSTQK LGSLNNEPAL PSTSYLPSTP SVVPASSYIP SSETPPAPSS REASRPPEEP SAPSPTLPAQ FKQRAPMYNS GLSPATPTPA APTSPLTPTT PPAVAPTTQT PPVAMVAPQT QAPAQQQPKK NLSLTREQMF AAQEMFKTAN KVTRPEKALI LGFMAGSREN PCQEQGDVIQ IKLSEHTEDL PKADGQGSTT MLVDTVFEMN YATGQWTRFK KYKPMTNVS.

    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.

    Whsc2 Human
  • View Data Sheet

    Name :

    BCL7C Human

    Description:

    B-cell CLL/lymphoma 7C Human Recombinant

    B-Cell CLL/Lymphoma 7C, B-Cell CLL/Lymphoma 7 Protein Family Member C, BCL7C.

    Product # :

    PRO-1781

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    Description

    BCL7C Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-217 a.a) and having a molecular mass of 25.9kDa (Molecular size on SDS-PAGE will appear higher).BCL7C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCL7C protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      B-cell CLL/lymphoma 7C (BCL7C) is identified by the likeness of its product to the N-terminal region of BCL7A protein. The BCL7A protein is encoded by the gene which is directly involved in a three-way gene translocation in a Burkitt lymphoma cell line. The function of the BCL7C gene has not been determined yet.

    • Synonyms

      B-Cell CLL/Lymphoma 7C, B-Cell CLL/Lymphoma 7 Protein Family Member C, BCL7C.

    • 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.

    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.

    Bcl7C Human
  • View Data Sheet

    Name :

    BMP 2 Human, HEK

    Description:

    Bone Morphogenetic protein-2 Human Recombinant, HEK

    BMP-2, BMP2A.

    Product # :

    CYT-080

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    Description

    BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

    Citations

    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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-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 BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 28kDa.

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

      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 specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

      What is the amino acid sequence of BMP2 Protein?
      QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.

      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 Hek
  • View Data Sheet

    Name :

    Leptin Super Antagonist Rat

    Description:

    Leptin Super Antagonist Rat Recombinant

    Product # :

    CYT-1240

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    Description

    Super Leptin Antagonist Rat Recombinant is a single polypeptide chain containing 146 amino acids. Super Rat Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super Rat leptin antagonist that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    Citations

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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

    Leptin Antagonist Super Rat
  • View Data Sheet

    Name :

    Myostatin Propeptide Human

    Description:

    Myostatin Propeptide Human Recombinant

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

    Product # :

    CYT-448

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    Description

    Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized with no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.

    Citations

    More Info

    • Introduction

      Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.

    • Synonyms

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

    • Physical Appearance

      Sterile 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.

    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
  • View Data Sheet

    Name :

    Bartonella 26kDa

    Description:

    Bartonella Henselae 26kDa Recombinant

    Product # :

    PRO-2569

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    Description

    Recombinant Bartonella Henselae 26kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 25kDa. Bartonella 26kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bartonella 26kDa is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.

      Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.

      Bartonella henselae of outer membrane protein p26 has an important nucleotide identity with orthologs in Bartonella spp, Brucella spp in addition to more than a few plant-associated bacteria.

    • 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. Avoid multiple freeze-thaw cycles.

    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.

    Bartonella Henselae 26Kda
  • View Data Sheet

    Name :

    RBKS Human

    Description:

    Ribokinase Human Recombinant

    Ribokinase, RBKS, RBSK, DKFZp686G13268.

    Product # :

    PKA-358

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    Description

    RBKS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 342 amino acids (1-322 a.a.) and having a molecular mass of 36.3kDa. The RBKS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RBKS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ribokinase (RBKS) is a member of the pfkB family of carbohydrate kinases. Ribokinase phosphorylates ribose to form ribose-5-phosphate in the presence of ATP and magnesium as a first step in ribose metabolism.

    • Synonyms

      Ribokinase, RBKS, RBSK, DKFZp686G13268.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAASGEPQRQ WQEEVAAVVV VGSCMTDLVS LTSRLPKTGE TIHGHKFFIG FGGKGANQCV QAARLGAMTS MVCKVGKDSF GNDYIENLKQ NDISTEFTYQ TKDAATGTAS IIVNNEGQNI IVIVAGANLL LNTEDLRAAA NVISRAKVMV CQLEITPATS LEALTMARRS GVKTLFNPAP AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSAADAGEA ALVLLKRGCQ VVIITLGAEG CVVLSQTEPE PKHIPTEKVK AVDTTGAGDS FVGALAFYLA YYPNLSLEDM LNRSNFIAAV SVQAAGTQSS YPYKKDLPLT LF.

    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.

    Rbks Human
  • View Data Sheet

    Name :

    CNTF Human

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

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    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    Citations

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 HCNTF 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 Met-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

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

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

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 standard solution of CNTF Recombinant 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.

    Cntf Human
  • View Data Sheet

    Name :

    TROVE2 Bovine, Biotin

    Description:

    TROVE Domain Family Member 2 Human Recombinant, Biotinlyated

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-2561

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    Description

    TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

    Source

    Bovine tissues.

    Formulation

    TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 83.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • 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.

    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.

    Ro60 Bovine
  • 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 :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    Citations

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

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

    Leptin Human
  • View Data Sheet

    Name :

    LUM Mouse

    Description:

    Lumican Mouse Recombinant

    Lum, Ldc, SLRR2D, Lumican, Keratan sulfate proteoglycan lumican, KSPG lumican.

    Product # :

    PRO-2609

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    Description

    LUM Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 328 amino acids (19-338 a.a) and having a molecular mass of 37.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LUM is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LUM protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lumican also known as LUM is a part of the small leucine-rich proteoglycan (SLRP) family which comprises decorin, biglycan, fibromodulin, keratocan, epiphycan, and osteoglycin. Furthermore, we can see that in these bifunctional molecules, the protein moiety binds collagen fibrils and the highly charged hydrophilic glycosaminoglycans regulate interfibrillar spacings. Lumican is the main keratan sulfate proteoglycan of the cornea however LUM is also distributed in interstitial collagenous matrices throughout the body. Lumican regulates collagen fibril organization and circumferential growth, corneal transparency, epithelial cell migration and tissue repair.

    • Synonyms

      Lum, Ldc, SLRR2D, Lumican, Keratan sulfate proteoglycan lumican, KSPG lumican.

    • 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

      QYYDYDIPLF MYGQISPNCA PECNCPHSYP TAMYCDDLKL KSVPMVPPGI KYLYLRNNQI
      DHIDEKAFEN VTDLQWLILD LLENSKIK GKVFSKLKQL KKLHINYNNL TESVGPLPKS
      LQDLQLTNNK ISKLGSFDGL VNLTFIYLQH NQLKEDAVSA SLKGLKSLEY LDLSFNQMSK
      LPAGLPTSLL TLYLDNNKIS NIPDEYFKRF TGLQYLRLSH NELADSGVPG NSFNISSLLE
      LDLSYNKLKS IPTVNENLEN YYLEVNELEK FDVKSFCKIL GPLSYSKIKH LRLDGNPLTQ SSLPPDMYEC LRVANEITVN VEHHHHHH.

    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.

    Lumican Mouse
  • View Data Sheet

    Name :

    CCL5 Mouse

    Description:

    Rantes Mouse Recombinant (CCL5)

    Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    Product # :

    CHM-342

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    Description

    Rantes Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 68 amino acids and having a molecular mass of 7876 Dalton. The Mouse Rantes is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a solution in 2×PBS, pH7.4.

    Purity

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

    Biological Activity

    The activity is determined by the ability to chemoattract total human lymphocytes population at a concentration between 1-10ng/ml.

    Citations

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse Rantes although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL5 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 Rantes in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPYGSDTTPC CFAYLSLALP RAHVKEYFYT SSKCSNLAVV FVTRRNRQVC ANPEKKWVQE YINYLEMS.

    • Background

      What is the molecular weight/Mw of CCL5 MOUSE Protein?
      CCL5 MOUSE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL5 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL5 MOUSE Protein?
      CCL5 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL5 MOUSE Protein?
      The activity is determined by the ability to chemoattract total human lymphocytes population at a concentration between 1-10ng/ml.

      What is the amino acid sequence of CCL5 MOUSE Protein?
      SPYGSDTTPC CFAYLSLALP RAHVKEYFYT SSKCSNLAVV FVTRRNRQVC ANPEKKWVQE YINYLEMS.

      What applications can CCL5 MOUSE Protein be used in?
      CCL5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL5 MOUSE Protein?
      The endotoxin level is minimal, CCL5 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL5 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL5 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Rantes Mouse
  • View Data Sheet

    Name :

    Glycinin

    Description:

    Allergen Ara h 3.0101 Recombinant

    Glycinin, Arah3.

    Product # :

    ALR-008

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    Description

    Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

    • Synonyms

      Glycinin, Arah3.

    • 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 IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Glycinin
  • View Data Sheet

    Name :

    VEGF Human

    Description:

    Vascular Endothelial Growth Factor Human Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-241

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    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.

    Citations

    More Info

    • Introduction

      Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

    • Protein content

      VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 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 VEGF 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.

    Vegf Human
  • View Data Sheet

    Name :

    BCL2L11 Human

    Description:

    BCL2 Like 11 Human Recombinant

    Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.

    Product # :

    PRO-1171

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    Description

    BCL2L11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-138 a.a) and having a molecular mass of 18.5kDa.BCL2L11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    BCL2L11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 2M Urea, 20% glycerol, 5mM DTT and 300mM NaCl.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Bcl-2-like protein 11 (BCL2L11) is a member of the Bcl-2 family and contains a Bcl-2 homology domain 3 (BH3). BCL2L11 expression can be stimulated by nerve growth factor (NGF), in addition to the forkhead transcription factor (FKHR-L1) which proposes a role of the BCL2L11 gene in neuronal and lymphocyte apoptosis. BCL2L11 interacts with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and acts as an apoptotic activator. BimEL, BimL and BimS are the main isoforms which are ubiquitously expressed with a tissue-specific variation. The Isoform Bim-gamma, on the other hand, is most abundantly expressed in the small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney.

    • Synonyms

      Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.

    • 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 MGSHMAKQPS DVSSECDREG RQLQPAERPP QLRPGAPTSL QTEPQDRSPA PMSCDKSTQT PSPPCQAFNH YLSAMASMRQ AEPADMRPEI WIAQELRRIG DEFNAYYARR VFLNNYQAAE DHPRMVILRL LRYIVRLVWR MH.

    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.

    Bcl2L11 Human
  • View Data Sheet

    Name :

    Glucagon-Like Peptide1 Human

    Description:

    Human Glucagon Like Peptide-1

    GLP1, Glucagon Like Peptide-1, Incretin hormone.

    Product # :

    HOR-284

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • formulation
    • purity
    • More Info
    • Citations

    Description

    Glucagon Like Peptide-1 is a single, non-glycosylated, polypeptide chain containing 30 amino acids and having a molecular mass of 3297.7 Dalton.The GLP-1 is purified by proprietary chromatographic techniques.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 96.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
      GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
      GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.

    • Synonyms

      GLP1, Glucagon Like Peptide-1, Incretin hormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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 Glucagon Like Peptide-1 in sterile H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2.

    • Background

      What is the molecular weight/Mw of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
      GLUCAGON-LIKE PEPTIDE1 HUMAN Protein has a total Mw of 3.297kDa.

      What is the Purity of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
      GLUCAGON-LIKE PEPTIDE1 HUMAN Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
      The biological functionality of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
      H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2.

      What applications can GLUCAGON-LIKE PEPTIDE1 HUMAN Protein be used in?
      GLUCAGON-LIKE PEPTIDE1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
      The endotoxin level is minimal, GLUCAGON-LIKE PEPTIDE1 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies GLUCAGON-LIKE PEPTIDE1 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of GLUCAGON-LIKE PEPTIDE1 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Glp 1 Human
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