CCL3/MIP-1α Antibody [C14E20] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
10 kDa

Datasheet & SDS

Biological Description

Specificity
CCL3/MIP-1α Antibody [C14E20] detects endogenous levels of total CCL3/MIP-1α protein.

Clone
C14E20

Synonym(s)
C-C motif chemokine 3, C-C motif chemokine ligand 3, CCL3, G0/G1 switch regulatory protein 19-1, G0S19-1, LD78-alpha(4-69), LD78ALPHA, MIP-1-alpha, MIP-1-alpha(4-69), MIP1A, PAT 464.1, SCYA3, SIS-beta

Background
CCL3, also known as macrophage inflammatory protein‑1α (MIP‑1α), is a CC chemokine produced by activated macrophages, monocytes, T cells, NK cells, and other leukocytes, and functions as a potent mediator of inflammatory cell recruitment, hematopoietic regulation, and tissue remodeling through high-affinity interactions with the chemokine receptors CCR1 and CCR5 on responsive target cells. The mature secreted chemokine adopts the characteristic CC chemokine fold with an N‑terminal region that contains the CC motif required for receptor activation and a surface enriched in basic residues that supports binding to glycosaminoglycans, which concentrates CCL3 on endothelial and stromal surfaces and establishes haptotactic gradients that guide leukocyte chemotaxis. Engagement of CCR1 or CCR5 by CCL3 activates Gi-coupled signaling, leading to inhibition of adenylyl cyclase, mobilization of intracellular Ca²⁺, and activation of downstream ERK1/2, JNK, and p38 MAPK pathways, which drive integrin activation, cytoskeletal rearrangement, and actin polymerization required for firm adhesion and directed migration across endothelium toward inflammatory foci. These signaling events also induce transcription and secretion of additional proinflammatory mediators, including TNF‑α and IL‑6, and can upregulate expression of CCR1 and CCR5 themselves, creating feed-forward loops that amplify local inflammatory responses and sustain accumulation and activation of monocytes, neutrophils, T cells, and NK cells within inflamed tissues. At the level of hematopoiesis, CCL3 acts directly on hematopoietic stem and progenitor cells to inhibit stem cell proliferation while permitting or enhancing proliferation of more mature progenitor subsets, a property that underpins its designation as a stem cell inhibitor and links CCL3 signaling to the control of stem cell quiescence and niche homeostasis in bone marrow. In the context of hematologic malignancy, particularly acute and chronic leukemias and multiple myeloma, elevated CCL3 expression in the marrow microenvironment correlates with disease burden and contributes to leukemogenesis by maintaining an inflammatory milieu, modulating stem/progenitor dynamics, and regulating osteoclast differentiation and activity, which promotes bone resorption and supports tumor cell growth. Within bone, CCL3 drives osteoclastogenesis via CCR1/CCR5-dependent pathways and simultaneously suppresses osteoblast function through ERK-mediated downregulation of osteogenic transcription factors such as osterix, leading to decreased osteocalcin production, impaired mineralization, and uncoupling of bone resorption from bone formation, a mechanism that underlies myeloma-induced osteolytic disease. The chemokine also participates in neuroimmune regulation, where elevated CCL3 in the central nervous system impairs synaptic transmission and hippocampal plasticity and modifies memory performance, reflecting direct effects on neuronal and glial signaling in addition to its classical roles in leukocyte recruitment.

Background

CCL3, also known as macrophage inflammatory protein‑1α (MIP‑1α), is a CC chemokine produced by activated macrophages, monocytes, T cells, NK cells, and other leukocytes, and functions as a potent mediator of inflammatory cell recruitment, hematopoietic regulation, and tissue remodeling through high-affinity interactions with the chemokine receptors CCR1 and CCR5 on responsive target cells. The mature secreted chemokine adopts the characteristic CC chemokine fold with an N‑terminal region that contains the CC motif required for receptor activation and a surface enriched in basic residues that supports binding to glycosaminoglycans, which concentrates CCL3 on endothelial and stromal surfaces and establishes haptotactic gradients that guide leukocyte chemotaxis. Engagement of CCR1 or CCR5 by CCL3 activates Gi-coupled signaling, leading to inhibition of adenylyl cyclase, mobilization of intracellular Ca²⁺, and activation of downstream ERK1/2, JNK, and p38 MAPK pathways, which drive integrin activation, cytoskeletal rearrangement, and actin polymerization required for firm adhesion and directed migration across endothelium toward inflammatory foci. These signaling events also induce transcription and secretion of additional proinflammatory mediators, including TNF‑α and IL‑6, and can upregulate expression of CCR1 and CCR5 themselves, creating feed-forward loops that amplify local inflammatory responses and sustain accumulation and activation of monocytes, neutrophils, T cells, and NK cells within inflamed tissues. At the level of hematopoiesis, CCL3 acts directly on hematopoietic stem and progenitor cells to inhibit stem cell proliferation while permitting or enhancing proliferation of more mature progenitor subsets, a property that underpins its designation as a stem cell inhibitor and links CCL3 signaling to the control of stem cell quiescence and niche homeostasis in bone marrow. In the context of hematologic malignancy, particularly acute and chronic leukemias and multiple myeloma, elevated CCL3 expression in the marrow microenvironment correlates with disease burden and contributes to leukemogenesis by maintaining an inflammatory milieu, modulating stem/progenitor dynamics, and regulating osteoclast differentiation and activity, which promotes bone resorption and supports tumor cell growth. Within bone, CCL3 drives osteoclastogenesis via CCR1/CCR5-dependent pathways and simultaneously suppresses osteoblast function through ERK-mediated downregulation of osteogenic transcription factors such as osterix, leading to decreased osteocalcin production, impaired mineralization, and uncoupling of bone resorption from bone formation, a mechanism that underlies myeloma-induced osteolytic disease. The chemokine also participates in neuroimmune regulation, where elevated CCL3 in the central nervous system impairs synaptic transmission and hippocampal plasticity and modifies memory performance, reflecting direct effects on neuronal and glial signaling in addition to its classical roles in leukocyte recruitment.

References
https://pubmed.ncbi.nlm.nih.gov/27308309/ https://link.springer.com/rwe/10.1007/978-94-007-7696-8_27

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%