Search: 1000 results found for "Insulin-Like Growth Factor"

Description:

Recombinant Anti Human Tumor Necrosis Factor-Alpha

Product # :

ANT-599

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Description

Recombinant TNF-a Antibody is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). Recombinant TNF-a Antibody is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.

Source

CHO.

Formulation

The Recombinant TNF-a Antibody 53mg/ml solution contains 6.16 mg/ml of sodium chloride, 0.86 mg/ml of monobasic sodium phosphate dihydrate, 1.53 mg/ml of dibasic sodium phosphate dihydrate, 0.3 mg/ml of sodium citrate, 1.30 mg/ml of citric acidmonohydrate, 12 mg/ml of mannitol, 1mg/ml of polysorbate 80, pH-5.

Purity

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

Biological Activity

The EC₅₀ as determined by L929 cell proliferation assay for neutralization reaction between TNF-a Antibody and TNFA, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.2 X 10⁴EU/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesisand viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Physical Appearance
Clear and colorless solution.
Stability
Recombinant TNF-a Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE. DO NOT SHAKE.
Amino Acid Sequence
LIGHT CHAIN
DIQMTQSPSSLSASVGDRVTITCRASQGIRNYLAWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDF
TLTISSLQPEDVATYYCQRYNRAPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

HEAVY CHAIN
EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSAITWNSGHIDYADSVEGRFTISR
DNAKNSLYLQMNSLRAEDTAVYYCAKVSYLSTASSLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA
ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVD
KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD
ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM
HEALHNHYTQKSLSLSPGK.

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:

PMF1-BGLAP Human Recombinant

PMF1-BGLAP Readthrough, PMF1-BGLAP Protein, Polyamine-Modulated Factor 1, PMF1.

Product # :

PRO-1760

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Description

PMF1-BGLAP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211aa) and having a molecular mass of 26.2kDa.PMF1-BGLAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PMF1-BGLAP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
PMF1-BGLAP is a locus which represents naturally occurring read-through transcription between the neighboring polyamine-modulated factor 1 (PMF1) and bone gamma-carboxyglutamate Gla protein (BGLAP) genes on chromosome 1. There are multiple transcript variants encoding isoforms as a results of alternative splicing which share sequence identity with the upstream gene product, but they have a different C-termini because of frameshifts as opposed to the downstream gene coding sequence.
Synonyms
PMF1-BGLAP Readthrough, PMF1-BGLAP Protein, Polyamine-Modulated Factor 1, PMF1.
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 MGSMAEASSA NLGSGCEEKR HEGSSSESVP PGTTISRVKL LDTMVDTFLQ KLVAAGSYQR FTDCYKCFYQ LQPAMTQQIY DKFIAQLQTS IREEISDIKE EGNLEAVLNA LDKIVEEGKV RKEPAWRPSG IPEKDLHSVM APYFLQQRDT LRRHVQKQEA ENQQLADAVL AGRRQVEELQ LQVQAQQQAW QVRSPAVQSP AKVQPLCPSR RAAR

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:

Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant

Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.

Product # :

PRO-167

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Description

EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EEF1B2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 100mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Elongation factor 1-beta (EEF1B2) is a translation elongation factor. EEF1B2 is a guanine nucleotide exchange factor which is involved in the transfer of aminoacylated tRNAs to the ribosome. Both EEF1B2 and EEF1D stimulate the exchange of GDP bound to EEF1A to GTP.
Synonyms
Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.
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
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKILEHHH HHH.

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

Description:

Placental Lactogen Bovine Recombinant

Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

Product # :

CYT-511

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Description

Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Placental Lactogen Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.

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:

Retinol Binding Protein-5 Human Recombinant

Retinol-binding protein 5, Cellular retinol-binding protein III, CRBP-III, HRBPiso, RBP5, CRBP3, CRBPIII.

Product # :

CYT-650

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Description

RBP5 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 155 amino acids (1-135 a.a.) and having a molecular mass of 18.1kDa. The RBP5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RBP5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
RBP5 is a member of the Retinol-binding proteins family. Estimation of retinol-binding protein is used to determine visceral protein mass in nutritional studies related to health. RBP5 has a higher expression in the adult kidney and liver and to a lesser extent in the adult and fetal spleen, adult lymph nodes and appendix, and fetal liver and kidney. RBP5 expression is strongly decreased in hepatocellular carcinoma tissues.
Synonyms
Retinol-binding protein 5, Cellular retinol-binding protein III, CRBP-III, HRBPiso, RBP5, CRBP3, CRBPIII.
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 MPPNLTGYYR FVSQKNMEDY LQALNISLAV RKIALLLKPD KEIEHQGNHM TVRTLSTFRN YTVQFDVGVE FEEDLRSVDG RKCQTIVTWE EEHLVCVQKG EVPNRGWRHW LEGEMLYLEL TARDAVCEQV FRKVR.

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:

RANK Ligand Soluble Mouse Recombinant

Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.

Product # :

CYT-320

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Description

sRANKL Mouse Recombinant produced in E.coli is single, non-glycosylated, polypeptide chain containing 174 amino acids ( 143-316 a.a.) and having a total molecular mass of 19.9kDa. CD254 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized with 10mM Na2PO4, pH 7.5 & 50mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to induce osteoclast formation on murine RAW264.7 cells using a concentration of 50ng/ml shown in “Corning® Osteo Assay Surface 24 Well Plates with Transwell® Permeable Supports- A Useful Tool for Co-Culture Studies” by Rebecca M. Wood and Mark Rothenber, corresponding to a specific activity of 20,000Units/mg.

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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
PAMMEGSWLD VAQRGKPEAQ PFAHLTINAA SIPSGSHKVT LSSWYHDRGW AKISNMTLSN GKLRVNQDGF YYLYANICFR HHETSGSVPT DYLQLMVYVV KTSIKIPSSH NLMKGGSTKN WSGNSEFHFY SINVGGFFKL RAGEEISIQV SNPSLLDPDQ DATYFGAFKV QDID.

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-11 Mouse Recombinant

AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

Product # :

CYT-646

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Description

Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

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Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
Synonyms
AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.

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:

Leptin Quadruple Antagonist Pegylated Mouse Recombinant

Product # :

CYT-1244

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Description

Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Angiopoietin-like Protein 7 Human Recombinant

angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein

Product # :

CYT-1208

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Description

ANGPTL7 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-346a.a) containing 553amino acids and having a molecular mass of 63.2kDa.ANGPTL7 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

ANGPTL7 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.
Synonyms
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 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
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
Background
Angiopoietin-like Protein 7 Human Recombinant: An Emerging Player in Metabolic Regulation and Therapeutic Potential
Abstract:
Angiopoietin-like protein 7 (ANGPTL7) is a multifunctional protein that has recently gained attention for its potential role in metabolic regulation and as a therapeutic target for metabolic disorders. ANGPTL7 is involved in the modulation of lipid metabolism, adipogenesis, and insulin signaling. The availability of human recombinant ANGPTL7 protein has provided researchers with a valuable tool to unravel its biological functions and explore its therapeutic applications. This review provides an overview of the current knowledge on ANGPTL7 and discusses its potential as a therapeutic intervention in metabolic disorders.
Introduction:
Metabolic disorders, including obesity and type 2 diabetes, pose significant health challenges worldwide. ANGPTL7, a member of the angiopoietin-like protein family, has recently emerged as a potential regulator of metabolic processes. ANGPTL7 affects lipid metabolism, adipose tissue biology, and insulin signaling pathways, making it an intriguing target for therapeutic interventions in metabolic disorders.
Role of ANGPTL7 in Metabolic Regulation:
ANGPTL7 plays a multifaceted role in metabolic regulation. It influences lipid metabolism by regulating lipoprotein lipase (LPL) activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL7 also affects adipocyte biology and adipogenesis, potentially contributing to the development of obesity and related metabolic complications. Furthermore, ANGPTL7 modulates insulin signaling and glucose metabolism, suggesting its involvement in insulin resistance and diabetes pathogenesis.
Mechanisms of ANGPTL7 Action:
ANGPTL7 exerts its effects through various mechanisms. It interacts with extracellular matrix components, influencing cell adhesion and migration. ANGPTL7 also regulates angiogenesis and vascular remodeling, potentially linking it to metabolic regulation and tissue homeostasis.
Therapeutic Potential of ANGPTL7 Human Recombinant Protein:
The availability of ANGPTL7 human recombinant protein offers new avenues for therapeutic interventions in metabolic disorders. Modulating ANGPTL7 activity through recombinant protein administration or targeted interventions may have significant implications for lipid metabolism, adipose tissue function, and insulin sensitivity. Exploring ANGPTL7 as a therapeutic target holds promise for the development of novel strategies to tackle metabolic disorders.
Conclusion:
ANGPTL7 is an emerging player in metabolic regulation with potential therapeutic implications for metabolic disorders. Its involvement in lipid metabolism, adipose tissue biology, and insulin signaling pathways highlights its importance in maintaining metabolic homeostasis. The availability of ANGPTL7 human recombinant protein opens up new possibilities for further investigations and the development of targeted interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL7 Protein?
ANGPTL7 Protein has a total Mw of 63.2kDa.

What is the source or expression system of ANGPTL7 Protein?
HEK293 cells.

What is the Purity of ANGPTL7 Protein?
ANGPTL7 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL7 Protein?
The biological functionality of ANGPTL7 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL7 Protein?
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

What applications can ANGPTL7 Protein be used in?
ANGPTL7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL7 Protein?
The endotoxin level is minimal, ANGPTL7 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:

Growth Arrest-Specific 7 Isoform b Human Recombinant

GAS7, GAS-7, Growth arrest-specific protein 7, KIAA0394, MGC1348, MLL/GAS7.

Product # :

PRO-680

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Quantity :

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source
formulation
purity
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Description

GAS7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-416a.a.) and having a molecular mass of 49.8 kDa.GAS7 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GAS7 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GAS7 is mainly expressed in terminally differentiated brain cells and predominantly in mature cerebellar Purkinje neurons. GAS7 is involved in neuronal development by promoting maturation and morphological differentiation of cerebellar neurons. Inhibition of GAS7 production in terminally differentiating cultures of embryonic murine cerebellum impedes neurite outgrowth. Over-expression of GAS7 initiats the development of human osteosarcoma.
Synonyms
GAS7, GAS-7, Growth arrest-specific protein 7, KIAA0394, MGC1348, MLL/GAS7.
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 MKPGMVPPPP GEESQTVILP PGWQSYLSPQ GRRYYVNTTT NETTWERPSS SPGIPASPGS HRSSLPPTVN GYHASGTPAH PPETAHMSVR KSTGDSQNLG SSSPSKKQSK ENTITINCVT FPHPDTMPEQ QLLKPTEWSY CDYFWADKKD PQGNGTVAGF ELLLQKQLKG KQMQKEMSEF IRERIKIEED YAKNLAKLSQ NSLASQEEGS LGEAWAQVKK SLADEAEVHL KFSAKLHSEV EKPLMNFREN FKKDMKKCDH HIADLRKQLA SRYASVEKAR KALTERQRDL EMKTQQLEIK LSNKTEEDIK KARRKSTQAG DDLMRCVDLY NQAQSKWFEE MVTTTLELER LEVERVEMIR QHLCQYTQLR HETDMFNQST VEPVDQLLRK VDPAKDRELW VREHKTGNIR PVDMEI.

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:

IFN Gamma Receptor 1 Human Recombinant

IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.

Product # :

CYT-1074

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Quantity :

Shipping Method :

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Description

IFNGR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (18-245a.a.) and having a molecular mass of 26.6kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IFNGR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IFNGR1 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
IFNGR1 is a part of the hematopoietic cytokine receptor superfamily. IFNGR1 forms a site that is recognized by the extracellular domain of IFNGR2 by inducing the rapid dimerization of chains. IFNGR1 Plays an important role in the IFN-gamma pathway that is essential for the cellular response to infectious agents. IFNGR1 is expressed in a membrane-bound form in various cells, and is over-expressed in tumor cells.
Synonyms
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
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
EMGTADLGPS SVPTPTNVTI ESYNMNPIVY WEYQIMPQVP VFTVEVKNYG VKNSEWIDAC INISHHYCNI SDHVGDPSNS LWVRVKARVG QKESAYAKSE EFAVCRDGKI GPPKLDIRKE EKQIMIDIFH PSVFVNGDEQ EVDYDPETTC YIRVYNVYVR MNGSEIQYKI LTQKEDDCDE IQCQLAIPVS SLNSQYCVSA EGVLHVWGVT TEKSKEVCIT IFNSSIKGHH HHHH.
Background
What is the molecular weight/Mw of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein has a total Mw of 16.8kDa.

What is the source or expression system of IFNGR1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNGR1 HUMAN Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

What is the amino acid sequence of IFNGR1 HUMAN Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.

What applications can IFNGR1 HUMAN Protein be used in?
IFNGR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNGR1 HUMAN Protein?
The endotoxin level is minimal, IFNGR1 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:

Inositol Hexakisphosphate Kinase 2 Human Recombinant

Inositol hexakisphosphate kinase 2 isoform a, IHPK2, PIUS, InsP6 kinase 2, P(i)-uptake stimulator, PiUS, IP6K2, TCCCIA00113.

Product # :

PKA-067

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Description

IP6K2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 446 amino acids (1-426a.a) and having a molecular mass of 51.3kDa.IP6K2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IP6K2 solution (0.5mg/ml) contains Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Inositol Hexakisphosphate Kinase 2 (IP6K2) which is a part of the inositol IPK family converts inositol hexakisphosphate to diphosphoinositol pentakisphosphate. IP6K2 also converts 1, 3, 4, 5, 6-pentakisphosphate (InsP5) to PP-InsP4. IP6K2 is a protein coding gene which suppresses the growth and affects the apoptotic activities of IFN-beta in several ovarian cancers.
Synonyms
Inositol hexakisphosphate kinase 2 isoform a, IHPK2, PIUS, InsP6 kinase 2, P(i)-uptake stimulator, PiUS, IP6K2, TCCCIA00113.
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 MSPAFRAMDV EPRAKGVLLE PFVHQVGGHS CVLRFNETTL CKPLVPREHQ FYETLPAEMR KFTPQYKGVV SVRFEEDEDR NLCLIAYPLK GDHGIVDIVD NSDCEPKSKL LRWTTNKKHH VLETEKTPKD WVRQHRKEEK MKSHKLEEEF EWLKKSEVLY YTVEKKGNIS SQLKHYNPWS MKCHQQQLQR MKENAKHRNQ YKFILLENLT SRYEVPCVLD LKMGTRQHGD DASEEKAANQ IRKCQQSTSA VIGVRVCGMQ VYQAGSGQLM FMNKYHGRKL SVQGFKEALF QFFHNGRYLR RELLGPVLKK LTELKAVLER QESYRFYSSS LLVIYDGKER PEVVLDSDAE DLEDLSEESA DESAGAYAYK PIGASSVDVR MIDFAHTTCR LYGEDTVVHE GQDAGYIFGL QSLIDIVTEI SEESGE.

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:

Growth Hormone Anatagonist Rat Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-1250

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Rat Growth Hormone Anatagonist produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. GH Antagonist Rat is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

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

Purity

Greater than 98.0% as determined by:

(a) Analysis by RP-HPLC

(b) Analysis by Gel Filtration.

(c) Analysis by SDS-PAGE.

Biological Activity

Plays a role as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain and binds to this ECD with affinity similar the the wild type rGH.

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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH Antagonist Rat although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 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 GH Antagonist Rat in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Ala-Met.
Background
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with 4 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 was evolved by a series of gene duplications. The 5 genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the 5 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 4 genes in the growth hormone locus.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman analysis program of protein sequences.

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:

CTLA4 Human Recombinant, igG-His Tag, Active

CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

Product # :

CYT-1144

Price :

Quantity :

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Description

CTLA4 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161aa) and having a molecular mass of 40.8kDa.CTLA4 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The CTLA4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Determined by the IL-2 ELISA in a using Jurkat human acute T cell leukemia cells. ED50 range for this is ≤ 150 ng/ml with Human B7 1/CD80.

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Introduction
Cytotoxic T-lymphocyte-associated protein 4 or CTLA4 or CD152 is a receptor that takes part in the immune checkpoint and inhibits immune response. This protein is fundamentally found in regulatory T cells; however, it acts as an enhancer in regular T cells following its activation, this is eminent in cancers. CTLA4 bounds to CD80 or CD86 on the membrane of antigen presenting cells and downregulates transductions.
Synonyms
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
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
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG
NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI
DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD
VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN
KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH
Background
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 40.8kDa.

What is the source or expression system of CTLA4 Protein?
Sf9, Baculovirus cells.

What is the Purity of CTLA4 Protein?
CTLA4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTLA4 Protein?
Determined by the IL-2 ELISA in a using Jurkat human acute T cell leukemia cells. ED50 range for this is ≤ 150 ng/ml with Human B7 1/CD80.

What is the amino acid sequence of CTLA4 Protein?
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG
NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI
DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD
VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN
KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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-7 Human Recombinant

Osteogenic Protein 1, BMP-7.

Product # :

CYT-333

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton. The BMP-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-7 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.

Purity

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

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, BMP-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in 20mM-100mM acetic acid at a concentration of 0.1-0.5mg per ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Thr-Gly-Ser-Lys.
Background
Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review
Abstract:
Bone Morphogenetic Protein-7 (BMP-7) is a crucial member of the transforming growth factor-beta (TGF-β) superfamily with diverse roles in development, tissue repair, and regeneration.
This research paper provides a comprehensive review of BMP-7 Human Recombinant, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of BMP-7 modulation.
Introduction:
BMP-7 is a multifunctional growth factor that plays a significant role in skeletal development and tissue homeostasis. This paper aims to provide an extensive review of BMP-7 Human Recombinant, highlighting its importance in various biological processes and its potential therapeutic applications.
Structure and Function of BMP-7:
BMP-7 is a disulfide-linked homodimeric protein composed of two subunits. It binds to specific cell surface receptors, activating downstream signaling pathways, including the Smad pathway and non-Smad signaling cascades. These pathways regulate cellular processes such as proliferation, differentiation, and apoptosis.
Skeletal Development and Regeneration:
BMP-7 is a key regulator of bone formation and remodeling. It promotes osteoblast differentiation and bone mineralization, contributing to skeletal development and repair. BMP-7 also plays a role in cartilage formation and chondrogenesis.
Tissue Repair and Regeneration:
Beyond its skeletal functions, BMP-7 is involved in tissue repair and regeneration in various organs, including the kidney, liver, and heart. It promotes the regeneration of damaged tissues by stimulating cell proliferation, angiogenesis, and extracellular matrix remodeling.
Therapeutic Potential:
Due to its regenerative and reparative properties, BMP-7 has attracted significant attention as a potential therapeutic agent. It has been investigated for its applications in bone regeneration, cartilage repair, and the treatment of kidney and liver diseases. Clinical trials exploring the therapeutic efficacy of BMP-7 are ongoing.
Challenges and Future Perspectives:
Despite the promising therapeutic potential of BMP-7, challenges remain, including optimizing its delivery systems, understanding its dosage and duration of treatment, and managing potential side effects. Future research should focus on unraveling the intricate mechanisms of BMP-7 signaling, developing targeted therapies, and enhancing its clinical applications.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 15kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.

What is the amino acid sequence of BMP7 Protein?
BMP7 Protein is composed from 139 amino acids.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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 Alpha Porcine Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

Product # :

CYT-396

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin-1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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 IL-1 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.

Description:

Small EDRK-Rich Factor 2 Human Recombinant

Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

Product # :

PRO-1730

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.
Synonyms
Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.
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 MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK

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:

LIGHT Human Recombinant

Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light

Product # :

CYT-1202

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

Recombinant Human LIGHT (74-240 aa) having a Mw of 23kDa was purified from E. coli.The Recombinant Human LIGHT is purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

TNFSF14 solution contains PBS & 25mM K2CO3.

Purity

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

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light
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
DGPAGSWEQL IQERRSHEVN PAAHLTGANS SLTGSGGPLL WETQLGLAFL RGLSYHDGAL VVTKAGYYYI YSKVQLGGVG CPLGLASTIT HGLYKRTPRY PEELELLVSQ QSPCGRATSS SRVWWDSSFL GGVVHLEAGE KVVVRVLDER LVRLRDGTRS YFGAFMV

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:

Leptin Quadruple Antagonist Pegylated Ovine Recombinant

Product # :

CYT-1246

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Description

Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

SMARCA4 Human Recombinant

SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.

Product # :

PRO-2071

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Description

SMARCA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (362-549aa) and having a molecular mass of 25kDa. SMARCA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SMARCA4 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.

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Introduction
SMARCA4 belongs to the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Proteins in this family have helicase and ATPase activities and are considered to regulate transcription ofcertain genes by altering the chromatin structure around those genes. SMARCA4 is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is essential for transcriptional activation of genesnormally repressed by chromatin. In addition, SMARCA4 is able to bind BRCA1, as well as regulating the expression ofthe tumorigenic protein CD44. Moreover, mutations in SMARCA4 cause rhabdoid tumor predisposition syndrome type 2.
Synonyms
SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.
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 MGSDPVEILQ EREYRLQARI AHRIQELENL PGSLAGDLRT KATIELKALR LLNFQRQLRQ EVVVCMRRDT ALETALNAKA YKRSKRQSLR EARITEKLEK QQKIEQERKR RQKHQEYLNS ILQHAKDFKE YHRSVTGKIQ KLTKAVATYH ANTEREQKKE NERIEKERMR RLMAEDEEGY RKLIDQKKDK R.

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:

CD30 Ligand Receptor Human Recombinant

Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

Product # :

CYT-927

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Description

TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 370 amino acids (19-379 a.a.) and having a molecular mass of 39.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TNFRSF8 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF8 protein solution (1mg/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
Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.
Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.
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
ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKHHHHHH.

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:

Placental Lactogen Caprine Recombinant

Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

Product # :

CYT-510

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Shipped at Room temp

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Description

Placental Lactogen Caprine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant Goat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Placental Lactogen Caprine is biologically active as evidenced by inducing proliferation of Nb2 cells.

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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Goat is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized caprine recombinant placental lactogen although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of caprine recombinant placental lactogen at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization caprine recombinant placental lactogen can be stored at 4C for several weeks.
Solubility
It is recommended to reconstitute the lyophilized caprine recombinant placental lactogen in sterile water or 0.4% NaHCO3 adjusted tp pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
Amino Acid Sequence
The sequence of the first four N-terminal amino acids was determined and was found to be Ala-Glu-Asn-Tyr.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.85 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.

Description:

Galectin-2 Mouse Recombinant

Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.

Product # :

CYT-019

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SDS-PAGE

Description

LGALS2 mouse Recombinant produced E. coli is a single polypeptide chain containing 153 amino acids (1-130) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LGALS2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.
Synonyms
Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.
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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
Background
What is the molecular weight/Mw of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein has a total Mw of 17.3kDa.

What is the source or expression system of LGALS2 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS2 MOUSE Protein?
The biological functionality of LGALS2 MOUSE Protein will be determined in the future.

What is the amino acid sequence of LGALS2 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

What applications can LGALS2 MOUSE Protein be used in?
LGALS2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS2 MOUSE Protein?
The endotoxin level is minimal, LGALS2 MOUSE 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:

Mouse Anti Human Dickkopf-Related Protein 3

Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

Product # :

ANT-707

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formulation
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Formulation

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

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Introduction
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.
Synonyms
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human DKK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human DKK3 protein (22-350 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT103B5AT.
Applications
DKK3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
DKK3 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.

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