Search: 1000 results found for "Lactoferrin"

Description:

Insulin-Like Growth Factor-1 Clone PAT6F8AT, Mouse Anti Human

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

Product # :

ANT-538

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Formulation

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

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the 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). Three 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 colorless solution.
Immunogen
Anti-human IGF1 mAb, clone PAT6F8AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IGF1 protein 49-118 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT6F8AT.
Applications
HSPA5 antibody has been tested by ELISA, 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 starting dilution is 1:1000.
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
IGF1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

Cyclophilin-F, Mouse Anti Human

Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

Product # :

ANT-389

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Formulation

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

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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Immunogen
Anti-human Cyclophilin-F mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cyclophilin-F amino acids 30-207 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT1F5AT.
Applications
Cyclophilin-F antibody has been tested by ELISA, Western blot and immunohistochemistry 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 is 1:500~1:1,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:500 and Immunohistochemistry is 1:50.
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
Cyclophilin-F 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.

Description:

Epstein Barr Virus Induced 3 Human Recombinant, His Tag

Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.

Product # :

CYT-668

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Description

EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 34kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 protein is supplied in 1xPBS, 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 34kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.

What is the amino acid sequence of EBI3 Protein?
EBI3 Protein is composed from 209 amino acids.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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.

Description:

Amelotin Human Recombinant

UNQ689, Amelotin, PRO1329.

Product # :

PRO-1301

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Description

AMTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (17-209 a.a.) and having a molecular mass of 22.2kDa.AMTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AMTN protein solution (0.5mg/ml) contains mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.
Synonyms
UNQ689, Amelotin, PRO1329.
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 MGSLPQLKPA LGLPPTKLAP DQGTLPNQQQ SNQVFPSLSL IPLTQMLTLG PDLHLLNPAA GMTPGTQTHP LTLGGLNVQQ QLHPHVLPIF VTQLGAQGTI LSSEELPQIF TSLIIHSLFP GGILPTSQAG ANPDVQDGSL PAGGAGVNPA TQGTPAGRLP TPSGTDDDFA VTTPAGIQRS THAIEEATTE SANGIQ.

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.

Description:

TRAIL Receptor-1 Human Recombinant

TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.

Product # :

CYT-1043

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Description

TNFRSF10A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 224 amino acids (24-239a.a.) and having a molecular mass of 23.9kDa. TNFRSF10A is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF10A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
Synonyms
TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.
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
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSEHPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSRGCPR GMVKVKDCTP WSDIECVHKE SGNGHNLEHH HHHH

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

Description:

Hemoglobin-Zeta Mouse Recombinant

Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.

Product # :

PRO-2517

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Description

HBZ Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a) and having a molecular mass of 18.3kDa.HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HBZ protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.
Synonyms
Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.
Physical Appearance
Sterile Filtered clear 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 MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP EVHEAWDKFM SILSSILTEK YR.

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.

Description:

Elongin B Mouse Recombinant

Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

Product # :

PRO-2550

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Description

ELOB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 141 amino acids ( 1-118 a.a.) having a molecular mass of 15.6 kDa. The Recombinant Mouse ELOB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains PBS pH-7.4 containing 1mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.
Synonyms
Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.
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 MGSMDVFLMI RRHKTTIFTD AKESSTVFEL KRIVEGILKR PPEEQRLYKD DQLLDDGKTL GECGFTSQTA RPQAPATVGL AFRADDTFEA LRIEPFSSPP ELPDVMKPQD SGGSANEQAV Q

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.

Description:

Interleukin-12 p35 Human Recombinant

NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

Product # :

CYT-487

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Description

Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

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.

Description:

Allergen Ara h 6.0101 Recombinant

Conglutin, Allergen Ara h 6.

Product # :

ALR-009

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Description

Recombinant Conglutin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 16,217 Dalton. Conglutin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Conglutin is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Conglutin, also known as Ara h 6.0101 is a part of the 2S albumin protein family. Conglutin along with Ara h 2.0201 are considered as some of the most potent elicitors of anaphylaxis. Both proteins hold multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure. Conglutin causes an allergic reaction in human and binds to IgE.
Synonyms
Conglutin, Allergen Ara h 6.
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.

Description:

Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

Product # :

CHM-323

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Description

SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

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.

Description:

Nuclear Receptor Binding Factor 2 Human Recombinant

Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.

Product # :

PRO-1692

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Description

NRBF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (45-287) and having a molecular mass of 29.9 kDa.NRBF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NRBF2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.
Synonyms
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
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 MGSMKLTQSE QAHLSLELQR DSHMKQLLLI QERWKRAQRE ERLKAQQNTD KDAAAHLQTS HKPSAEDAEG QSPLSQKYSP STEKCLPEIQ GIFDRDPDTL LYLLQQKSEP AEPCIGSKAP KDDKTIIEEQ ATKIADLKRH VEFLVAENER LRKENKQLKA EKARLLKGPI EKELDVDADF VETSELWSLP PHAETATASS TWQKFAANTG KAKDIPIPNL PPLDFPSPEL PLMELSEDIL KGFMNN.

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.

Description:

Insulin Like Growth Factor Binding Protein-7Human Recombinant, His Tag

Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

Product # :

CYT-809

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SDS-PAGE

Description

IGFBP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (27-282 a.a.) and having a molecular mass of 28.8kDa.IGFBP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGFBP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

Purity

Greater than 85% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.
Synonyms
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
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 MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.
Background
What is the molecular weight/Mw of IGFBP7 HUMAN, HIS Protein?
IGFBP7 HUMAN, HIS Protein has a total Mw of 28.8kDa.

What is the source or expression system of IGFBP7 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IGFBP7 HUMAN, HIS Protein?
IGFBP7 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP7 HUMAN, HIS Protein?
The biological functionality of IGFBP7 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IGFBP7 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.

What applications can IGFBP7 HUMAN, HIS Protein be used in?
IGFBP7 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP7 HUMAN, HIS Protein?
The endotoxin level is minimal, IGFBP7 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.

Description:

Bone Morphogenetic protein-3 Human Recombinant

Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

Product # :

CYT-937

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Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Description

BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

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Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.

What is the source or expression system of BMP3 Protein?
Escherichia Coli.

What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 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.

Description:

Killer Cell Lectin-Like Receptor Subfamily C, Member 1 Human Recombinant

NKG2-A/NKG2-B type II integral membrane protein isoform NKG2-A, KLRC1, Killer Cell Lectin-Like Receptor Subfamily C, Member 1, KLRC1, CD159A, NKG2, NKG2A, CD159 antigen-like family member A, NK cell receptor A, NKG2-A/B-activating NK receptor.

Product # :

PRO-2440

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Description

KLRC1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 149 amino acids (94-233a.a.) and having a molecular mass of 17.1kDa. KLRC1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

KLRC1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Killer Cell Lectin-Like Receptor Subfamily C, Member 1 (KLRC1) is a part of the killer cell lectin-like receptor family. KLRC1 functions as a receptor for the detection of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRC1 is also connects with CD94 and is expressed on NK cells and some activated T cell.
Synonyms
NKG2-A/NKG2-B type II integral membrane protein isoform NKG2-A, KLRC1, Killer Cell Lectin-Like Receptor Subfamily C, Member 1, KLRC1, CD159A, NKG2, NKG2A, CD159 antigen-like family member A, NK cell receptor A, NKG2-A/B-activating NK receptor.
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
ADPPSTLIQR HNNSSLNTRT QKARHCGHCP EEWITYSNSC YYIGKERRTW EESLLACTSK NSSLLSIDNE EEMKFLSIIS PSSWIGVFRN SSHHPWVTMN GLAFKHEIKD SDNAELNCAV LQVNRLKSAQ CGSSIIYHCK HKLHHHHHH

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.

Description:

Mannose-Binding Lectin 2 Human Recombinant, Sf9

Mannose Binding Lectin 2, Mannose-Binding Lectin (Protein C) 2, Soluble (Opsonic Defect), Collectin-1, COLEC1, MBP-C, MBP1, MBL, Mannose-Binding Lectin 2, Soluble (Opsonic Defect), Mannose-Binding Lectin (Protein C) 2, Soluble, Mannose-Binding Protein C, Mannan-Binding Protein, Mannose-Binding Lectin, Mannan-Binding Lectin, HSMBPC, MBL2D, MBPD, MBP.

Product # :

PRO-2526

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Quantity :

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Shipped with Ice Packs

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Description

MBL2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 237 amino acids (21-248a.a.) and having a molecular mass of 25.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). MBL2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MBL2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Mannose-binding protein C (MBL2), belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.
Synonyms
Mannose Binding Lectin 2, Mannose-Binding Lectin (Protein C) 2, Soluble (Opsonic Defect), Collectin-1, COLEC1, MBP-C, MBP1, MBL, Mannose-Binding Lectin 2, Soluble (Opsonic Defect), Mannose-Binding Lectin (Protein C) 2, Soluble, Mannose-Binding Protein C, Mannan-Binding Protein, Mannose-Binding Lectin, Mannan-Binding Lectin, HSMBPC, MBL2D, MBPD, MBP.
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
ADPETVTCED AQKTCPAVIA CSSPGINGFP GKDGRDGTKG EKGEPGQGLR GLQGPPGKLG PPGNPGPSGS PGPKGQKGDP GKSPDGDSSL AASERKALQT EMARIKKWLT FSLGKQVGNK FFLTNGEIMT FEKVKALCVK FQASVATPRN AAENGAIQNL IKEEAFLGIT DEKTEGQFVD LTGNRLTYTN WNEGEPNNAG SDEDCVLLLK NGQWNDVPCS TSHLAVCEFP IHHHHHH

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.

Description:

SYF2 RNA splicing factor Human Recombinant

Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.

Product # :

PRO-969

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Quantity :

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Description

SYF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (94-243) and having a molecular mass of 20.5kDa.SYF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SYF2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Pre-mRNA-splicing factor SYF2 (SYF2) may be involved in pre-mRNA splicing. The SYF2 protein interacts with cyclin D-type binding-protein 1, which is believed to be a cell cycle regulator at the G1/S transition. SYF2 is amply expressed in the heart, skeletal muscle and kidney and is expressed at lower levels in other tissues.
Synonyms
Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.
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 MGSDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV.

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.

Description:

Fibroblast Growth Factor Basic 147 a.a. Human Recombinant

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-557

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Quantity :

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Shipped at Room temp

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x10⁷ units/mg.

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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb 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 FGF-B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 16.5kDa.

What is the source or expression system of FGF 2 Protein?
Escherichia Coli.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

What is the amino acid sequence of FGF 2 Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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.

Description:

Protein L Cys Recombinant

Product # :

PRO-1931

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Quantity :

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Shipped at Room temp

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description
source
formulation
purity
More Info
sds-page, HPLC

Description

Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

Source

Escherichia Coli.

Formulation

Protein-L was lyophilized without any additives.

Purity

Greater than 96.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

sds-page, HPLC

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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.

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.

Description:

Adiponectin (108-244 a.a.) Human Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-073

Price :

Quantity :

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Shipped with Ice Packs

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sds-page

Description

Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..

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

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

Description:

Insulin-Like Growth Factor Binding Protein-7 Human Recombinant

Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

Product # :

CYT-788

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Recombinant Human IGFBP7 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 2x256 amino acid chains and having a molecular mass of 26.4kDa. The IGFBP-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IGFBP7 was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.

Purity

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

More Info

Introduction
Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.
Synonyms
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFBP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-7 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 IGFBP-7 in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL.
Background
What is the molecular weight/Mw of IGFBP7 HUMAN Protein?
IGFBP7 HUMAN Protein has a total Mw of 26.4kDa.

What is the source or expression system of IGFBP7 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGFBP7 HUMAN Protein?
IGFBP7 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP7 HUMAN Protein?
The biological functionality of IGFBP7 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IGFBP7 HUMAN Protein?
SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL.

What applications can IGFBP7 HUMAN Protein be used in?
IGFBP7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP7 HUMAN Protein?
The endotoxin level is minimal, IGFBP7 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.

Description:

Beta Defensin-1 Human Recombinant

Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

Product # :

CYT-564

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Description

Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.

Purity

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

Biological Activity

Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

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Synonyms
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
Background
Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications
Abstract:

Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.
Introduction:

Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.
BD-1 Structure and Function:

BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.
Antimicrobial Properties and Therapeutic Applications:

BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.
Therapeutic Potential of BD-1 Human Recombinant:

BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.
Challenges and Future Directions:

While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.
Conclusion:

BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 5kDa.

What is the source or expression system of BD1 Protein?
Escherichia Coli.

What is the Purity of BD1 Protein?
BD1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD1 Protein?
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

What is the amino acid sequence of BD1 Protein?
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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.

Description:

Interleukin-1 Receptor Antagonist Rat Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

Product # :

CYT-152

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Description

IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL 1RA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ

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.

Description:

Interleukin-6 Mouse Recombinant, His Tag

Interleukin-6, IL-6.

Product # :

CYT-845

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Description

Interleukin-6 Mouse Recombinant produced in E.Coli migrates at 25kDa. Recombinant IL-6 Mouse is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

IL6 Mouse protein solution contains 25mM K2CO3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
Interleukin-6, IL-6.
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.
Background
Research Paper on Interleukin-6 Mouse Recombinant, His Tag
Abstract:
Interleukin-6 (IL-6) Mouse Recombinant, tagged with His, is a cornerstone in unraveling the intricate web of immune modulation. This research paper delves into its molecular intricacies and its profound implications in immunological research. Through an exploration of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its pivotal role in shaping immune responses.
Introduction:
IL-6 Mouse Recombinant, bearing a His tag, has emerged as a pivotal tool in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.
Molecular Features and His Tag Precision:
Unveiling the molecular structure of IL-6 Mouse Recombinant, His Tag, we recognize its significance in facilitating purification and characterization. The His tag enhances our ability to study its functions with precision.
Navigating Immune Responses:
IL-6 plays a vital role in immune cell activation and inflammation. IL-6 Mouse Recombinant, His Tag, enables researchers to delve deeper into the cytokine's functions, shedding light on its impact on immune dynamics.
Synonyms and Network Connections:
Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of cytokine-mediated signaling networks. IL-6 Mouse Recombinant, His Tag, contributes to our understanding of these interconnected pathways.
Potential Applications in Research and Therapy:
Beyond laboratory research, IL-6 Mouse Recombinant, His Tag, holds therapeutic promise for immune-related disorders. Its utility in investigating disease mechanisms and evaluating therapeutic interventions marks it as a versatile tool.
Clinical Implications and Future Avenues:
The clinical relevance of IL-6 Mouse Recombinant, His Tag, is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its potential as a therapeutic intervention opens avenues for novel treatment strategies.
Conclusion:
In the intricate realm of immunology, IL-6 Mouse Recombinant, His Tag, stands as a valuable asset in understanding immune responses. Its molecular precision, pivotal functions, and potential therapeutic implications position it as an indispensable tool for advancing our knowledge of immune regulation.

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.

Description:

Recombinant Human Interleukin 10 Receptor Beta

Interleukin-10 receptor subunit beta, IL-10 receptor subunit beta, IL-10R subunit beta, IL-10RB, Cytokine receptor class-II member 4, Cytokine receptor family 2 member 4, CRF2-4, Interleukin-10 receptor subunit 2, IL-10R subunit 2, IL-10R2, CDw210b, IL10RB.

Product # :

CYT-1025

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Description

IL10RB Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 440 amino acids (20-220 a.a.) and having a molecular mass of 50.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL10RB is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL10RB protein solution (1.0mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
Interleukin-10 receptor subunit beta, IL-10 receptor subunit beta, IL-10R subunit beta, IL-10RB, Cytokine receptor class-II member 4, Cytokine receptor family 2 member 4, CRF2-4, Interleukin-10 receptor subunit 2, IL-10R subunit 2, IL-10R2, CDw210b, IL10RB.
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
MVPPPENVRM NSVNFKNILQ WESPAFAKGN LTFTAQYLSY RIFQDKCMNT TLTECDFSSL SKYGDHTLRV RAEFADEHSD WVNITFCPVD DTIIGPPGMQ VEVLADSLHM RFLAPKIENE YETWTMKNVY NSWTYNVQYW KNGTDEKFQI TPQYDFEVLR NLEPWTTYCV QVRGFLPDRN KAGEWSEPVC EQTTHDETVP SLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

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.

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