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Search results

1000 results found for “Glucagon”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    Leptin Human

    Description:

    Human Leptin

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

    Product # :

    CYT-683

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • formulation
    • purity
    • More Info
    • Citations

    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.

    Citations

    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 :

    BGN Human, Sf9

    Description:

    Biglycan Human Recombinant, Sf9

    BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    Product # :

    PRO-2536

    Price :

    Quantity :

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    • Citations

    Description

    BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic  fibroblast  adipose-like cells.

    Citations

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    • 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

      ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.

    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.

    Biglycan Human
  • View Data Sheet

    Name :

    Leptin Salamander

    Description:

    Leptin Salamander Recombinant

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

    Product # :

    CYT-704

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
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    • More Info
    • Citations

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.

    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, Leptin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.

    • Solubility

      It is recommended to reconstitute the lyophilized Salamander 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

      The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 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 Salamander
  • View Data Sheet

    Name :

    XG Human

    Description:

    XG Blood Group Human Recombinant

    Glycoprotein Xg isoform 1 precursor, PBDX, Glycoprotein Xg, PBDX, XG.

    Product # :

    PRO-1395

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    XG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (22-142a.a) and having a molecular mass of 15.5kDa. XG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    XG protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      XG is the XG blood group antigen, and is at the pseudoautosomal boundary on the short (p) arm of chromosome X. The three 5' exons are located in the pseudoautosomal area and the remaining exons within the X-specific end. A shorted copy of XG is found on the Y chromosome at the pseudoautosomal boundary. XG is transcribed, although not expected to make a Y-chromosome specific gene product.

    • Synonyms

      Glycoprotein Xg isoform 1 precursor, PBDX, Glycoprotein Xg, PBDX, XG.

    • 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 MGSQRDFDLA DALDDPEPTK KPNSDIYPKP KPPYYPQPEN PDSGGNIYPR PKPRPQPQPG NSGNSGGYFN DVDRDDGRYP PRPRPRPPAG GGGGGYSSYG NSDNTHGGDH HSTYGNPEGN MVAK.

    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.

    Xg Human
  • View Data Sheet

    Name :

    HbA1c Human

    Description:

    Human Hemoglobin A1c

    Product # :

    PRO-299

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • Citations

    Description

    The Human Hemoglobin A1c was purified from Human Erythrocytes.

    Source

    Human Erythrocytes.

    Formulation

    The HbA1c is supplied in a proprietary buffer formulation having pH-8.0. The HbA1c was dispensed on the basis of HbA1c not total hemoglobin.

    Purity

    Greater than 96.0%.

    Citations

    More Info

    • Introduction

      The HbA1c shows the average amount of glucose in the blood over a period of 3 months. Sugar in the bloodstream can become attached to the hemoglobin in red blood cells (glycosylation). Once the sugar is attached, it stays there for the life of the red blood cell, which is about 120 days. The higher the level of blood sugar, the more sugar attaches to red blood cells. The HbA1c is formed in a non-enzymatic pathway by hemoglobin's standard exposure to elevated plasma levels of glucose. HbA1c is tested to monitor nephropathy and retinopathy in diabetes mellitus.

    • Physical Appearance

      Clear red frozen solution.

    • Stability

      Human HbA1c although stable at 4°C for 1 week, should be stored at -20°C.

    • Human Virus Test

      Tissue sample tested and found negative for HIV-1 & 2 antibodies, HBsAg, and Hepatitis-C antibodies.

    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.

    Hba1C Human
  • View Data Sheet

    Name :

    Ipamorelin

    Description:

    Ipamorelin

    Ipamorelin

    Product # :

    HOR-024

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • Citations

    Description

    Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Introduction

      Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.

    • Synonyms

      Ipamorelin

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Aib-His-D-2-Nal-D-Phe-Lys-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.

    Ipamorelin
  • View Data Sheet

    Name :

    CALN1 Human

    Description:

    Calnueron-1 Human Recombinant

    Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.

    Product # :

    PRO-279

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    Description

    CALN1 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 212 amino acids (1-192 a.a.) and having a molecular mass of 24kDa. The CALN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALN1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 50mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CALN1 is highly similar to the calcium-binding proteins of the calmodulin family. The CALN1 protein contains two EF-hand domains and potential calcium-binding sites. Also, CALN1 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 has a role in the physiology of neurons and is potentially significant in memory and learning.

    • Synonyms

      Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.

    • 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 MPFHHVTAGL LYKGNYLNRS LSAGSDSEQL ANISVEELDE IREAFRVLDR DGNGFISKQE LGMAMRSLGY MPSEVELAII MQRLDMDGDG QVDFDEFMTI LGPKLVSSEG RDGFLGNTID SIFWQFDMQR ITLEELKHIL YHAFRDHLTM KDIENIIINE EESLNETSGN CQTEFEGVHS QKQNRQTCVR KS.

    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.

    Caln1 Human
  • View Data Sheet

    Name :

    Humanin

    Description:

    Humanin

    Product # :

    HOR-042

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    Description

    Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Humanin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Humanin 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 Humanin 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-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.

    • Background

      Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.

      Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.

      Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.

      Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).

      Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.

      The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.

    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.

    Humanin
  • View Data Sheet

    Name :

    IGF1 Human, A67T

    Description:

    Insulin Like Growth Factor-1, Mutant A67T Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    CYT-1089

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    Description

    IGF1 A67T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa. The IGF1 A67T is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IGF1 A67T Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 6.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IGF1 A67T in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

    • Background

      What is the molecular weight/Mw of IGF1 HUMAN, A67T Protein?
      IGF1 HUMAN, A67T Protein has a total Mw of 7.7kDa.

      What is the source or expression system of IGF1 HUMAN, A67T Protein?
      Escherichia Coli.

      What is the Purity of IGF1 HUMAN, A67T Protein?
      IGF1 HUMAN, A67T Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 HUMAN, A67T Protein?
      The biological functionality of IGF1 HUMAN, A67T Protein will be determined in the future.

      What is the amino acid sequence of IGF1 HUMAN, A67T Protein?
      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

      What applications can IGF1 HUMAN, A67T Protein be used in?
      IGF1 HUMAN, A67T Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 HUMAN, A67T Protein?
      The endotoxin level is minimal, IGF1 HUMAN, A67T 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.

    Igf1 A67T
  • View Data Sheet

    Name :

    pGH 22kDa Human

    Description:

    Growth Hormone Placental 22kDa Human Recombinant

    GHL, GHV, GH-V, hGH-V, PGH.

    Product # :

    CYT-235

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    Description

    Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.

    Purity

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

    Citations

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GHL, GHV, GH-V, hGH-V, PGH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions 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 Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, 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 Ala-Phe-Pro-Thr-Ile.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 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 GH-22K-placental 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.

    Placental Gh 22K Human
  • View Data Sheet

    Name :

    GSK3B Antibody

    Description:

    Glycogen synthase kinase-3 beta, Mouse Anti Human

    GSK3B, Glycogen synthase kinase-3 beta, GSK-3 beta.

    Product # :

    ANT-404

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    Formulation

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

    Citations

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    • Introduction

      GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

    • Synonyms

      GSK3B, Glycogen synthase kinase-3 beta, GSK-3 beta.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human GSK3B mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GSK3B amino acids 341-420 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1F7AT.

    • Applications

      GSK3B antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 3,000. Recommended starting dilution is 1:2,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      GSK3B antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Gsk3B Antibody
  • View Data Sheet

    Name :

    Triptorelin

    Description:

    Triptorelin Acetate

    Product # :

    HOR-238

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    Description

    Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

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

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

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

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

    Triptorelin
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    Citations

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    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 Brain-derived Neurotrophic Factor 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.

    Bdnf Human
  • View Data Sheet

    Name :

    Insulin Antibody

    Description:

    Insulin, Mouse Anti-Human

    Product # :

    ANT-100

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    Description

    These clones have been derived from hybridization of X63-Ag8-653 myeloma cells with spleen cells of Balb/c mice immunised with purified human insulin.

    Formulation

    The vial contains antibody in PBS, pH 7.4, containing 0.09% of sodium azide (NaN3) as preservative.

    Citations

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    • 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.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Store at + 4°C.

    • Clone

      7F8.

    • Species Reactivity

      These antibodies cross-react with human proinsulin, bovine insulin (30%) and porcine insulin. No cross-reaction with free C-peptide.

    • Specificity

      Insulin, human.

    • Isotype

      IgG1 kappa.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      Purified by chromatography on protein A chromatography.

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

    Insulin Antibody
  • View Data Sheet

    Name :

    S100G Human

    Description:

    S100 Calcium Binding Protein G Human Recombinant

    Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.

    Product # :

    PRO-156

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    Description

    The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    Citations

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    • Introduction

      S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.

    • Synonyms

      Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.

    • Applications

      Western blotting.

    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.

    S100G Human
  • View Data Sheet

    Name :

    AMBP

    Description:

    Alpha-1 Microglobulin Human Recombinant

    Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin, uronic-acid-rich protein.

    Product # :

    PRO-957

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    Description

    AMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (20-203) and having a molecular mass of 23.1 kDa.AMBP is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
      A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
      Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
      Alpha-1-microglobulin was first discovered in pathological human urine.
      It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

    • Synonyms

      Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin,
      uronic-acid-rich protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGPVPTPPDN IQVQENFNIS RIYGKWYNLA IGSTCPWLKK IMDRMTVSTL VLGEGATEAE ISMTSTRWRK GVCEETSGAY EKTDTDGKFL YHKSKWNITM ESYVVHTNYD EYAIFLTKKF SRHHGPTITA KLYGRAPQLR ETLLQDFRVV AQGVGIPEDS IFTMADRGEC VPGEQEPEPI LIPRV.

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    Ambp Human
  • View Data Sheet

    Name :

    ATG5 Human

    Description:

    Autophagy Related 5 Human Recombinant

    Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.

    Product # :

    PRO-454

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    Description

    ATG5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-275a.a.) and having a molecular mass of 34.6kDa.ATG5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATG5 at a concentration of 0.25mg/ml containing 20mM Tris-HCl, pH 8.0, 1mM DTT , 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

    • Synonyms

      Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.

    • 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 MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLPRVSYLTLVTD KVKKHFQKVM RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNITVHFKSFPEK DLLHCPSKDA IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLKEVCPSAIDPE DGEKKNQVMI HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD

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    Atg5 Human
  • View Data Sheet

    Name :

    GAGE2D Human

    Description:

    G Antigen 2D Human Recombinant

    G Antigen 2D, Cancer/Testis Antigen 4.8, CT4.8, GAGE-8, GAGE8, G Antigen 8.

    Product # :

    PRO-1726

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    Description

    GAGE2D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (1-116 a.a) and having a molecular mass of 15.2kDa (Molecular size on SDS-PAGE will appear higher).GAGE2D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GAGE2D protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GAGE2D is a member of the GAGE family, which organized in clustered repeats. In addition, they have a high degree of predicted sequence identity, but differ by scattered single nucleotide substitution. Thefirst GAGE nomenclature was based on identified mRNA sequences; however the high identity of the GAGE membersmade it impossible to separate products of paralogous genes from polymorph products. Moreover GAGE2D is not expressed in normal tissues, except in testis; however it is expressed by a large proportion of tumors of various histological origins.

    • Synonyms

      G Antigen 2D, Cancer/Testis Antigen 4.8, CT4.8, GAGE-8, GAGE8, G Antigen 8.

    • 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 MGSMSWRGRS TYRPRPRRYV EPPEMIGPMR PEQFSDEVEP ATPEEGEPAT QRQDPAAAQE GEDEGASAGQ GPKPEADSQE QGHPQTGCEC EDGPDGQEMD PPNPEEVKTP EEGEKQSQC

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    Gage2D Human
  • View Data Sheet

    Name :

    Procalcitonin Canine

    Description:

    Procalcitonin Canine Recombinant

    Calcitonin, Calca, Calc, CCALCI.

    Product # :

    HOR-015

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    Description

    Procalcitonin Canine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Arg130) containing 115 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 12.7kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 7.2.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc, CCALCI.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASAPFRSALEGL PDPTALSEKE GRLLLAALVK AYVQRKNELE QEQEQETEGS SLDSSRAKRC SNLSTCVLGT YSKDLNNFHT FSGIGFGAET PGKKRDIASG LERGR.

    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.

    Procalcitonin Canine
  • View Data Sheet

    Name :

    HAPLN1 Human

    Description:

    Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant

    Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    Product # :

    PRO-2012

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    Description

    HAPLN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (16-354 a.a.) and having a molecular mass of 40.9kDa.HAPLN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAPLN1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hyaluronan And Proteoglycan Link Protein 1, which is also known as HAPLN1 is a part of the HAPLN family.HAPLN1 contains one Ig-like V-type domain and two Link domains. In the extracellular cartilage matrix, HAPLN1 stabilizes the aggregates of proteoglycan monomers by means of hyaluronic acid .

    • Synonyms

      Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    • 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 MGSDHLSDNY TLDHDRAIHI QAENGPHLLV EAEQAKVFSH RGGNVTLPCK FYRDPTAFGS GIHKIRIKWT KLTSDYLKEV DVFVSMGYHK KTYGGYQGRV FLKGGSDSDA SLVITDLTLE DYGRYKCEVI EGLEDDTVVV ALDLQGVVFP YFPRLGRYNL NFHEAQQACL DQDAVIASFD QLYDAWRGGL DWCNAGWLSD GSVQYPITKP REPCGGQNTV PGVRNYGFWD KDKSRYDVFC FTSNFNGRFY YLIHPTKLTY DEAVQACLND GAQIAKVGQI FAAWKILGYD RCDAGWLADG SVRYPISRPR RRCSPTEAAV RFVGFPDKKH KLYGVYCFRA YN.

    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.

    Hapln1 Human
  • View Data Sheet

    Name :

    FUCA2 Human

    Description:

    Fucosidase Alpha-L- 2 Plasma Human Recombinant

    Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    Product # :

    ENZ-840

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    Description

    FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

    • Synonyms

      Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    • 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 MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.

    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.

    Fuca2 Human
  • View Data Sheet

    Name :

    CXCL9 Human, His

    Description:

    MIG Human Recombinant (CXCL9), His Tag

    C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.

    Product # :

    CHM-016

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    Description

    MIG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (23-125 a.a.) and having a molecular mass of 14kDa.MIG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MIG (CXCL9) is a small cytokine which is part of the CXC chemokine family. MIG, which is also recognized as monokine is induced by gamma interferon. MIG is related to 2 other CXC chemokines named CXCL10 and CXCL11, whose genes are located next to the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 obtain their chemotactic functions by interacting with the chemokine receptor CXCR3.

    • Synonyms

      C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.

    • 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 MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.

    • Background

      What is the molecular weight/Mw of CXCL9 HUMAN, HIS Protein?
      CXCL9 HUMAN, HIS Protein has a total Mw of 14kDa.

      What is the source or expression system of CXCL9 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL9 HUMAN, HIS Protein?
      CXCL9 HUMAN, HIS Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL9 HUMAN, HIS Protein?
      The biological functionality of CXCL9 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL9 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.

      What applications can CXCL9 HUMAN, HIS Protein be used in?
      CXCL9 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL9 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL9 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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

    Mig Human His
  • View Data Sheet

    Name :

    HPSE Human

    Description:

    Heparanase-1 Human Recombinant

    Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    Product # :

    ENZ-778

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    Description

    HPSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (36-543 a.a) and having a molecular mass of 60kDa.HPSE is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HPSE protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.

    • Synonyms

      Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    • 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 MGSQDVVDLD FFTQEPLHLV SPSFLSVTID ANLATDPRFL ILLGSPKLRT LARGLSPAYL RFGGTKTDFL IFDPKKESTF EERSYWQSQV NQDICKYGSI PPDVEEKLRL EWPYQEQLLL REHYQKKFKN STYSRSSVDV LYTFANCSGL DLIFGLNALL RTADLQWNSS NAQLLLDYCS SKGYNISWEL GNEPNSFLKK ADIFINGSQL GEDFIQLHKL LRKSTFKNAK LYGPDVGQPR RKTAKMLKSF LKAGGEVIDS VTWHHYYLNG RTATKEDFLN PDVLDIFISS VQKVFQVVES TRPGKKVWLG ETSSAYGGGA PLLSDTFAAG FMWLDKLGLS ARMGIEVVMR QVFFGAGNYH LVDENFDPLP DYWLSLLFKK LVGTKVLMAS VQGSKRRKLR VYLHCTNTDN PRYKEGDLTL YAINLHNVTK YLRLPYPFSN KQVDKYLLRP LGPHGLLSKS VQLNGLTLKM VDDQTLPPLM EKPLRPGSSL GLPAFSYSFF VIRNAKVAAC I.

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    Hpse Human
  • View Data Sheet

    Name :

    ARHGDIA Human

    Description:

    Rho GDP dissociation inhibitor (GDI) alpha Human Recombinant

    Rho GDP-dissociation inhibitor 1, Rho GDI 1, Rho-GDI alpha, ARHGDIA, GDIA1, RHOGDI, RHOGDI-1, MGC117248.

    Product # :

    PRO-002

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    Description

    ARHGDIA Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids (24-204 a.a.) and having a molecular mass of 22.9kDa. The ARHGDIA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Rho GDP-dissociation inhibitor 1 (ARHGDIA) is a member of the RAS gene superfamily, which encodes small guanine nucleotide exchange (GTP/GDP) factors. ARHGDIA, which is localized to the cytoplasm, inhibits the dissociation of GDP from Rho proteins, thus preventing GTP from binding to and consequently activating Rho proteins. In humans, the ARHGDIA can be phosphorylated at Ser 101 by p21-activated kinase, an event that inhibits its activity and may result in positive feedback regulation of several ARHGDIA target proteins.

    • Synonyms

      Rho GDP-dissociation inhibitor 1, Rho GDI 1, Rho-GDI alpha, ARHGDIA, GDIA1, RHOGDI, RHOGDI-1, MGC117248.

    • 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 MSVNYKPPAQ KSIQEIQELD KDDESLRKYK EALLGRVAVS ADPNVPNVVV TGLTLVCSSA PGPLELDLTG DLESFKKQSF VLKEGVEYRI KISFRVNREI VSGMKYIQHT YRKGVKIDKT DYMVGSYGPR AEEYEFLTPV EEAPKGMLAR GSYSIKSRFT DDDKTDHLSW EWNLTIKKDW KD.

    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.

    Arhgdia Human
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