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Search results

1000 results found for “Lipocalin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    LHRH Human

    Description:

    Luteinizing Hormone Releasing Hormone Human

    Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-261

    Price :

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    Description

    Lutenizing Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 10 amino acids and having a molecular mass of 1182.2 Dalton. The molecular formula is C55H75N17O13.C2H4O2. The CAS Number is 71447-49-9.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Gonadotropin-releasing hormone 1 (GNRH1), also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LHRH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LNRH 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 LHRH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The LHRH is also soluble in a 1% glacial acetic acid.

    • Amino Acid Sequence

      Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.

    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.

    Lhrh Human
  • View Data Sheet

    Name :

    Goserelin

    Description:

    Goserelin

    Product # :

    HOR-256

    Price :

    Quantity :

    Shipping Method :

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    Description

    Goserelin contains 10 amino acids Glu1-His2-Trp3-Ser4-Tyr5-D-Ser(tBu)6-Leu7-Arg8-Pro9-AzGly10-NH2 and having a molecular weight of 1269.43 Dalton.

    Formulation

    The Goserelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Goserelin is a hormone similar to the one normally released from the hypothalamus gland in the brain (GnRH super-agonist). It is used to treat for prostate and breast cancer.
      Goserelin decreases the amount of estrogen and testosterone by this treating endometriosis and cancer of the breast, and can help thin the uterus lining before surgery. Goserelin prevents the growth of tissue associated with endometriosis.
      Reducing the amount of testosterone is one way of treating prostate cancer.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Goserelin
  • View Data Sheet

    Name :

    L Selectin Human

    Description:

    L-selectin Human Recombinant

    L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    Product # :

    PRO-381

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    L-Selectin Human Recombinant is expressed in E. coli containing 294 amino acids 39-332 fused to an amino terminal hexahistidine tag, having a total molecular weight of 37.55kDa.

    Source

    Escherichia Coli.

    Formulation

    L-Sel is supplied in 1x PBS and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
      L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
      L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

    • Synonyms

      L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      L-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    L Selectin Human
  • View Data Sheet

    Name :

    NCALD Human

    Description:

    Neurocalcin Delta Recombinant Human

    Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    Product # :

    PRO-093

    Price :

    Quantity :

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    • description
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    • formulation
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    • More Info

    Description

    NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.

    • Synonyms

      Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.

    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.

    Ncald Human
  • View Data Sheet

    Name :

    CRYGC Human

    Description:

    Crystallin, Gamma C Human Recombinant

    Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    Product # :

    PRO-1095

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    CRYGC Human Recombinant produced in E. coli is a single polypeptide chain containing 198 amino acids (1-174) and having a molecular mass of 23.5kDa.CRYGC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CRYGC solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRYGC is a member of the beta/gamma-crystallin family. Mammalian lens crystallins are distributed into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Gamma-crystallins are a homogeneous group of extremely symmetrical, monomeric proteins usually missing connecting peptides and terminal extensions and are differentially regulated after early development. Three pseudogenes (gamma-E,F,G) and four gamma-crystallin genes (gamma-A,B,C,D) are structured in a genomic sector as a gene cluster. Gamma-crystallins are involved in cataract formation as a result of aging or mutations in specific genes. Mutations in CRYGC result in cataract Coppock-like (CCL) and cataract autosomal dominant (ADC).

    • Synonyms

      Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    • 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 MGSHMGKITF YEDRAFQGRS YETTTDCPNL QPYFSRCNSI RVESGCWMLY ERPNYQGQQY LLRRGEYPDY QQWMGLSDSI RSCCLIPQTV SHRLRLYERE DHKGLMMELS EDCPSIQDRF HLSEIRSLHV LEGCWVLYEL PNYRGRQYLL RPQEYRRCQD WGAMDAKAGS LRRVVDLY

    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.

    Crygc Human
  • View Data Sheet

    Name :

    NIP7 Human

    Description:

    Nuclear Import 7 Homolog Human Recombinant

    Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.

    Product # :

    PRO-780

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    Description

    NIP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-180 a.a.) and having a molecular mass of 21.5kDa. NIP7 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NIP7 protein solution contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.

    • Synonyms

      Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.

    • 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

      MRPLTEEETR VMFEKIAKYI GENLQLLVDR PDGTYCFRLH NDRVYYVSEK IMKLAANISG DKLVSLGTCFGKFTKTHKFR LHVTALDYLA PYAKYKVWIK PGAEQSFLYG NHVLKSGLGR ITENTSQYQG VVVYSMADIPLGFGVAAKST QDCRKVDPMA IVVFHQADIG EYVRHEETLT LEHHHHHH.

    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.

    Nip7 Human
  • View Data Sheet

    Name :

    CPLX1 Human

    Description:

    Complexin-1 Human Recombinant

    CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    Product # :

    PRO-645

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    Description

    CPLX1 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 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90% by SDS-PAGE.

    More Info

    • Introduction

      CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.

    • Synonyms

      CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    • 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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.

    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.

    Cplx1 Human
  • View Data Sheet

    Name :

    Cyclophilin A Mouse

    Description:

    Cyclophilin A Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    Product # :

    ENZ-857

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    Description

    Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    • 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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.

    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.

    Cyclophilin A Mouse
  • View Data Sheet

    Name :

    Leptin Human

    Description:

    Human Leptin

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.

    Product # :

    CYT-683

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    Description

    Leptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.

    Formulation

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

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    More Info

    • Introduction

      A 16kDa 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, Leptin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature, should be stored desiccated below -20°C. Reconstituted Leptin is best stored refrigerated at 4°C.

    • Solubility

      The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

    • Amino Acid Sequence

      Val-Pro-Ile-Gln-Lys-Val-Gln-Asp-Asp-Thr-Lys-Thr-Leu-Ile-Lys-Thr-Ile-Val-Thr-Arg-Ile-Asn-Asp-Ile-Ser-His-Thr-Gln-Ser-Val-Ser-Ser-Lys-Gln-Lys.

    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 Synthetic
  • View Data Sheet

    Name :

    Leptin Pufferfish

    Description:

    Leptin Pufferfish Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-530

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    Description

    Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

    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 Pufferfish 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

      GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

      QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

    • Protein content

      Protein quantitation was carried out by 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).

    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 Pufferfish
  • View Data Sheet

    Name :

    Leptin Rat, PEG

    Description:

    Pegylated Rat Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-592

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    Description

    Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by Gel-Filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    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 pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin 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 pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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 Rat Pegylated
  • 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.

    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 :

    Fertirelin

    Description:

    Fertirelin

    Product # :

    HOR-037

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    Description

    Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.

    • Background

      Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.

      Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.

      Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).

      In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.

      The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.

    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.

    Fertirelin
  • View Data Sheet

    Name :

    Borrelia Spielmanii DbpA

    Description:

    Borrelia Spielmanii Decorin Binding Protein A Recombinant

    Product # :

    BOR-026

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    Description

    Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa. Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

    • 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- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Spielmanii Dbpa
  • View Data Sheet

    Name :

    Leptin Ovine

    Description:

    Leptin Ovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-239

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    Description

    Leptin Ovine 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 SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    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 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-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.2 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 calibrated solution of Leptin Ovine 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.

    Leptin Ovine
  • View Data Sheet

    Name :

    Secretin Human

    Description:

    Secretin Human

    Product # :

    HOR-273

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    • More Info

    Description

    Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Secretin Human
  • View Data Sheet

    Name :

    Exenatide

    Description:

    Exenatide

    Exendin-4.

    Product # :

    HOR-246

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    • description
    • formulation
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    Description

    Exenatide is a single, non-glycosylated, peptide containing 39 amino acids and having a molecular mass of 4186.6 Dalton. Exenatide has the empirical formula C184H282N50O60S.

    Formulation

    The Exenatide peptide was lyophilized from a concentrated solution with no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Exenatide Derived from the saliva of the gila monster, is a 39 amino acid peptide that mimics the GLP-1 incretin, an insulin secretagogue with glucoregulatory effects. Typical responses to exenatide include improvements in the initial rapid release of endogenous insulin, suppression of glucagon release by the pancreas, regulation of gastric empyting, and reduced appetite - all of which function to lower blood glucose. Exenatide is self-regulating in that it lowers blood sugar when levels are elevated but does not continue to lower blood sugar when levels return to normal, unlike with sulfonylureas or insulins.

    • Synonyms

      Exendin-4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Exenatide
  • View Data Sheet

    Name :

    SIGLEC9 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 9 Human Recombinant

    Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.

    Product # :

    PRO-2447

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    Description

    SIGLEC9 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 573 amino acids (18-348a.a.) and having a molecular mass of 63.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SIGLEC9 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SIGLEC9 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 9 (SIGLEC9) is a member of the sialic acid-binding Ig-like lectin family, which is a part of the immunoglobulin superfamily expressed mostly on human blood leukocytes. SIGLEC9 is a Putative adhesion molecule which is expressed in bone marrow, placenta, spleen, and fetal liver. SIGLEC9 is also a part of the recently characterized CD33-related Siglec family of sialic acid binding protein.

    • Synonyms

      Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.

    • 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

      ADPQTSKLLT MQSSVTVQEG LCVHVPCSFS YPSHGWIYPG PVVHGYWFRE GANTDQDAPV ATNNPARAVW EETRDRFHLL GDPHTKNCTL SIRDARRSDA GRYFFRMEKG SIKWNYKHHR LSVNVTALTH RPNILIPGTL ESGCPQNLTC SVPWACEQGT PPMISWIGTS VSPLDPSTTR SSVLTLIPQP QDHGTSLTCQ VTFPGASVTT NKTVHLNVSY PPQNLTMTVF QGDGTVSTVL GNGSSLSLPE GQSLRLVCAV DAVDSNPPAR LSLSWRGLTL CPSQPSNPGV LELPWVHLRD AAEFTCRAQN PLGSQQVYLN VSLQSKATSG VTQGLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.

    Siglec9 Human
  • View Data Sheet

    Name :

    MED7 Human

    Description:

    Mediator Complex Subunit 7 Human Recombinant

    Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.

    Product # :

    PRO-1319

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    Description

    MED7 Human Recombinant produced in E. coli is a single polypeptide chain containing 256 amino acids (1-233) and having a molecular mass of 29.7 kDa.MED7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MED7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.

    • Synonyms

      Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.

    • 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 MGSMGEPQQV SALPPPPMQY IKEYTDENIQ EGLAPKPPPP IKDSYMMFGN QFQCDDLIIR PLESQGIERL HPMQFDHKKE LRKLNMSILI NFLDLLDILI RSPGSIKREE KLEDLKLLFV HVHHLINEYR PHQARETLRV MMEVQKRQRL ETAERFQKHL ERVIEMIQNC LASLPDDLPH SEAGMRVKTE PMDADDSNNC TGQNEHQREN SGHRRDQIIE KDAALCVLID EMNERP

    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.

    Med7 Human
  • View Data Sheet

    Name :

    Glucagon Human

    Description:

    Glucagon Human Recombinant

    GLP1, GLP2, GRPP.

    Product # :

    HOR-237

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    Description

    Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton. The Glucagon is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of recombinant Glucagon was formulated with 100mg of lactose.

    Purity

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

    Biological Activity

    The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

    More Info

    • Introduction

      Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
      Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

    • Synonyms

      GLP1, GLP2, GRPP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Glucagon although stable at room temperature for 3 weeks, should be stored at 40C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Solubility

      It is recommended to reconstitute the lyophilized Glucagon sterile 18MΩ-cm H2O not less than 100 µg/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 His-Ser-Gln-Gly-Thr.

    • Background

      What is the molecular weight/Mw of GLUCAGON HUMAN Protein?
      GLUCAGON HUMAN Protein has a total Mw of 3.48kDa.

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

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

      What is the Biological Activity of GLUCAGON HUMAN Protein?
      The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

      What is the amino acid sequence of GLUCAGON HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.

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

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

    Glucagon Human Recombinant
  • View Data Sheet

    Name :

    Betacellulin His Human

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

    Product # :

    CYT-077

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    • sds-page

    Description

    BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    Betacellulin-sds-page - Product image 1

    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.

    • Synonyms

      Betacellulin, Probetacellulin.

    • 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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 11.3kDa.

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

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

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

      What is the amino acid sequence of BETACELLULIN Protein?
      MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

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

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

    Btc His Human
  • View Data Sheet

    Name :

    Tri a 14.0101

    Description:

    Non-Specific Lipid-Transfer Protein Tri a 14 Recombinant

    Non-specific lipid-transfer protein, ltp142.

    Product # :

    ALR-025

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    Description

    Recombinant Non-Specific Lipid-Transfer Protein Tri a 14 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 13kDa. Tri a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Tri a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tri a 14.0101 is a non-specific lipid transfer protein and a major wheat allergen. Those who are sensitive to this allergen may have baker’s asthma, a frequent occupational allergic disease caused mainly by inhalation of cereal flour, especially wheat flour. Tri a 14.0101 consists of 4 helical fragments and irregular C-terminal regions which are highly stable to heat treatment and proteolytic attack.

    • Synonyms

      Non-specific lipid-transfer protein, ltp142.

    • 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 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.

    Tri A 140101
  • View Data Sheet

    Name :

    NCL Human

    Description:

    Nucleolin Human Recombinant

    Nucleolin, Protein C23, NCL, C23.

    Product # :

    PRO-1508

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    Description

    Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.

    • Synonyms

      Nucleolin, Protein C23, NCL, C23.

    • 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.

    Ncl Human
  • View Data Sheet

    Name :

    Leptin Ovine, MTS

    Description:

    Leptin Ovine Recombinant, MTS tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-531

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    Description

    Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    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 Ovine MTS tagged 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 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ovine Mts
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